The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane
K03070
-
-
2.129e-248
796.0
LZS3_k127_2207225_1
it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box) 5'-TTATC CA A CA A-3'. DnaA binds to ATP and to acidic phospholipids
Negative regulator of class I heat shock genes (grpE- dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons
K03705
-
-
0.00000000000000000000000000001368
128.0
LZS3_k127_2207225_11
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB
K03550
-
3.6.4.12
0.0000000000000000000000001932
113.0
LZS3_k127_2207225_14
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ
K03687
-
-
0.000000000000000004109
90.0
LZS3_k127_2207225_15
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA
K07042
-
-
0.00000000000005419
80.0
LZS3_k127_2207225_17
Prokaryotic N-terminal methylation motif
-
-
-
0.00000000001839
76.0
LZS3_k127_2207225_18
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE
K03695
-
-
0.0000000003778
72.0
LZS3_k127_2207225_19
Transcriptional regulator
-
-
-
0.0000001393
61.0
LZS3_k127_2207225_2
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7 L12 stalk, and near the tRNA binding site of the peptidyltransferase center
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome
K02874
-
-
0.00000000000000000000000000000000000000000004305
164.0
LZS3_k127_2685174_6
ABC-2 type transporter
K01992
-
-
0.0000000000000000000000000000000000007728
149.0
LZS3_k127_2685174_7
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit
K02994
-
-
0.00000000000000000000000000002314
121.0
LZS3_k127_2685174_8
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase
An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and or decay
Responsible for synthesis of pseudouridine from uracil
K06180
-
5.4.99.23
0.00000000000000000000000000000005643
138.0
LZS3_k127_3052264_26
Nucleotidyl transferase AbiEii toxin, Type IV TA system
-
-
-
0.00000000000000000000000000000005966
132.0
LZS3_k127_3052264_27
domain protein
K06881
-
3.1.13.3,3.1.3.7
0.0000000000000000000000000000001084
136.0
LZS3_k127_3052264_28
Cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally Phe) residue
K02654
-
3.4.23.43
0.0000000000000000000000000000003193
135.0
LZS3_k127_3052264_29
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides
K03624
-
-
0.000000000000000000000000000009792
123.0
LZS3_k127_3052264_3
In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons
K03625
-
-
0.000000000000000000000000004171
115.0
LZS3_k127_3052264_34
SMART Elongator protein 3 MiaB NifB
K06936
-
-
0.0000000000000000000000000085
121.0
LZS3_k127_3052264_35
Binds to the 23S rRNA
K02939
-
-
0.000000000000000000000000555
109.0
LZS3_k127_3052264_36
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO
K06187
-
-
0.0000000000000000000000008886
111.0
LZS3_k127_3052264_38
Zincin-like metallopeptidase
-
-
-
0.00000000000000000000002687
104.0
LZS3_k127_3052264_39
Belongs to the small heat shock protein (HSP20) family
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP)
K00762
-
2.4.2.10
0.0000000005824
68.0
LZS3_k127_3052264_51
-
-
-
-
0.0000000008558
61.0
LZS3_k127_3052264_52
Belongs to the bacterial ribosomal protein bL33 family
K02913
-
-
0.0000000009091
61.0
LZS3_k127_3052264_53
-
-
-
-
0.0000000009855
60.0
LZS3_k127_3052264_54
protein MJ0014 - Methanococcus jannaschii gi 1590824 gb AAB97992.1 (U67460) conserved
K07450
-
-
0.0000000162
64.0
LZS3_k127_3052264_56
radical SAM
K06871
-
-
0.000004406
57.0
LZS3_k127_3052264_57
Antitoxin Phd_YefM, type II toxin-antitoxin system
-
-
-
0.00006125
48.0
LZS3_k127_3052264_58
Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family
K03428,K07003,K15984
-
2.1.1.11,2.1.1.242
0.00006241
52.0
LZS3_k127_3052264_59
ParE toxin of type II toxin-antitoxin system, parDE
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis
K02358
-
-
8.345e-195
614.0
LZS3_k127_3964351_1
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF- independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism
Catalyzes the oxidation of 5,10- methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10- formyltetrahydrofolate
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome
Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase. Has low thioredoxin activity in vitro
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity
Catalyzes the reductive methylation of 2'-deoxyuridine- 5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction proline is first activated by ATP to form Pro- AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys- tRNA(Pro) is not edited by ProRS
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre- crRNA and tracrRNA of type II CRISPR loci if present in the organism
ATPase, P-type (transporting), HAD superfamily, subfamily IC
K01533,K17686
-
3.6.3.4,3.6.3.54
2.306e-217
697.0
LZS3_k127_429535_1
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner
signal transduction protein containing a membrane domain, an EAL and a GGDEF domain
-
-
-
0.000000000000000000000000000007309
130.0
LZS3_k127_429535_24
23S rRNA-intervening sequence protein
-
-
-
0.0000000000000000000000000004696
117.0
LZS3_k127_429535_25
Glycosyltransferase like family 2
K07011
-
-
0.000000000000000000003299
107.0
LZS3_k127_429535_26
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation
Catalyzes a two-step reaction, first charging an arginine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner
K02469
-
5.99.1.3
5.452e-265
840.0
LZS3_k127_4829014_1
Catalyzes the conversion of GDP-D-mannose to GDP-4- dehydro-6-deoxy-D-mannose
Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines
K05540
-
-
0.000000000000000000000000000000000003237
152.0
LZS3_k127_4829014_13
dUTP biosynthetic process
K01494
-
3.5.4.13
0.000000000000000000000000000009562
124.0
LZS3_k127_4829014_14
-
-
-
-
0.0000000000000000004935
98.0
LZS3_k127_4829014_16
sulfuric ester hydrolase activity
-
-
-
0.00000000001128
78.0
LZS3_k127_4829014_2
Catalyzes the two-step NADP-dependent conversion of GDP- 4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln)
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P)
Part of the ABC transporter FtsEX involved in asymmetric cellular division facilitating the initiation of sporulation
K09811
-
-
0.0000000000000000000000000000000001942
143.0
LZS3_k127_4955106_11
Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism
K03111
-
-
0.000000000000000000000000000000002014
134.0
LZS3_k127_4955106_12
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity
Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair
K01356
-
3.4.21.88
0.00000000000000006576
89.0
LZS3_k127_5552058_42
G5 domain
-
-
-
0.0000000000000008731
88.0
LZS3_k127_5552058_43
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln)
Could be involved in insertion of integral membrane proteins into the membrane
K08998
-
-
0.0000000000000000000000165
102.0
LZS3_k127_5615633_7
stage II sporulation protein
K06381
-
-
0.0000000000000004596
91.0
LZS3_k127_5615633_8
Acetyltransferase (GNAT) domain
-
-
-
0.00000000000001619
80.0
LZS3_k127_5615633_9
Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane
K03980
-
-
0.0000000000004391
72.0
LZS3_k127_5620288_0
General secretory system II protein E domain protein
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate
K03701
-
-
0.0
1146.0
LZS3_k127_5695175_1
damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage
K03702
-
-
1.046e-253
798.0
LZS3_k127_5695175_10
PFAM Glycosyl transferase, group 1
-
-
-
0.0000000000000000000000000000000000000000007017
173.0
LZS3_k127_5695175_11
GDP-mannose mannosyl hydrolase activity
K03574
-
3.6.1.55
0.000000000000000000000000000000000000124
145.0
LZS3_k127_5695175_12
Endonuclease containing a URI domain
K07461
-
-
0.0000000000000000000000000000000002978
136.0
LZS3_k127_5695175_13
Protein of unknown function (DUF4012)
-
-
-
0.00000000000000000000000000000573
139.0
LZS3_k127_5695175_14
PFAM Uncharacterised protein family UPF0047
-
-
-
0.00000000000000000002986
95.0
LZS3_k127_5695175_15
Signal Transduction Histidine Kinase
-
-
-
0.000000000000000008308
87.0
LZS3_k127_5695175_16
phosphatases
K01091
-
3.1.3.18
0.0000000000000002263
87.0
LZS3_k127_5695175_17
Domain of unknown function (DUF378)
K09779
-
-
0.0000000000000003401
80.0
LZS3_k127_5695175_19
NYN domain
-
-
-
0.0000002999
60.0
LZS3_k127_5695175_2
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr)
Copper binding proteins, plastocyanin/azurin family
-
-
-
0.0002093
49.0
LZS3_k127_5695175_3
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision
Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell
-
-
-
0.00000000000000000000000000000000000004031
169.0
LZS3_k127_5756745_12
Histidine kinase
-
-
-
0.00000000000000000000000000000000000005782
162.0
LZS3_k127_5756745_13
PemK-like, MazF-like toxin of type II toxin-antitoxin system
K07171
-
-
0.0000000000000000000000000000000000002358
143.0
LZS3_k127_5756745_14
Thioredoxin
-
-
-
0.000000000000000000000000000000000009925
150.0
LZS3_k127_5756745_15
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins
Nucleotidyl transferase AbiEii toxin, Type IV TA system
-
-
-
0.000000000000000000000000000003859
127.0
LZS3_k127_5756745_21
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit
Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter
K04078
-
-
0.000000000000000000000003924
104.0
LZS3_k127_5756745_23
23S rRNA-intervening sequence protein
-
-
-
0.00000000000000000000004964
102.0
LZS3_k127_5756745_24
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell
-
-
-
0.00000000000000000000008252
117.0
LZS3_k127_5756745_25
Transposase
-
-
-
0.000000000000000000002411
100.0
LZS3_k127_5756745_26
PFAM Divergent PAP2 family
K09775
-
-
0.00000000000000000006941
95.0
LZS3_k127_5756745_27
Sugar-specific transcriptional regulator TrmB
-
-
-
0.0000000000000001283
89.0
LZS3_k127_5756745_28
Transfers the N-acyl diglyceride group on what will become the N-terminal cysteine of membrane lipoproteins
Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction the enzyme is irreversibly inactivated
K00567
-
2.1.1.63
0.000000000000008867
78.0
LZS3_k127_5756745_34
-
-
-
-
0.00000000000005955
89.0
LZS3_k127_5756745_35
endonuclease containing a URI domain
K07461
-
-
0.000000000001609
71.0
LZS3_k127_5756745_36
COG3209 Rhs family protein
-
-
-
0.000000000001919
83.0
LZS3_k127_5756745_37
Concanavalin A-like lectin/glucanases superfamily
-
-
-
0.00000000000864
81.0
LZS3_k127_5756745_38
This protein specifically catalyzes the removal of signal peptides from prolipoproteins
K03101
-
3.4.23.36
0.00000000003225
67.0
LZS3_k127_5756745_39
Domain of unknown function
K20276
-
-
0.0000000001769
76.0
LZS3_k127_5756745_4
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins
Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA)
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin
Involved in formation and maintenance of cell shape
K03570
-
-
0.0000000000000003885
88.0
LZS3_k127_5879624_8
Involved in DNA repair and RecF pathway recombination
K03584
-
-
0.00000000003629
72.0
LZS3_k127_5879624_9
Ferredoxin
K05337
-
-
0.0000000001154
64.0
LZS3_k127_5957387_0
type I restriction modification DNA specificity domain
K01154,K03427
-
2.1.1.72,3.1.21.3
0.0
1020.0
LZS3_k127_5957387_1
amino acids such as threonine, to avoid such errors, it has a posttransfer editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner
K01873
-
6.1.1.9
6.838e-256
811.0
LZS3_k127_5957387_10
Metal dependent phosphohydrolases with conserved 'HD' motif.
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex
Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA
K04066
-
-
0.000000000000000000000000000000000000000881
169.0
LZS3_k127_5957387_23
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome
K02948
-
-
0.0000000000000000000000000000000000008033
145.0
LZS3_k127_5957387_24
Belongs to the universal ribosomal protein uS9 family
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre- initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initation complex
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain
K01872
-
6.1.1.7
1.081e-196
631.0
LZS3_k127_5957387_40
Belongs to the bacterial ribosomal protein bL36 family
K02919
-
-
0.0000000001279
63.0
LZS3_k127_5957387_41
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance
K02897
-
-
0.00000000000000000000001199
109.0
LZS3_k127_7250982_25
Hydrolase, P-loop family
K06925
-
-
0.00000000000000000000002233
104.0
LZS3_k127_7250982_26
Transposase IS200 like
-
-
-
0.00000000000000000000002782
105.0
LZS3_k127_7250982_27
PFAM ubiE COQ5 methyltransferase family
-
-
-
0.00000000000000000000003503
106.0
LZS3_k127_7250982_28
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site
Catalyzes the reversible conversion of 2- phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine)
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR)
-
-
-
0.0006389
51.0
LZS3_k127_7250982_6
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity
Catalyzes the conversion of GlcNAc-PP-undecaprenol into ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate in the de novo synthesis of teichoic acid
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu)
Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate
K11175
-
2.1.2.2
0.000000000000000000000000000000001248
139.0
LZS3_k127_7586514_11
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine
K01611
-
4.1.1.50
0.000000000000000001022
90.0
LZS3_k127_7586514_12
PemK-like, MazF-like toxin of type II toxin-antitoxin system
K07171
-
-
0.000000000000000002989
89.0
LZS3_k127_7586514_13
-
-
-
-
0.0000000000000003898
85.0
LZS3_k127_7586514_14
metal-dependent phosphohydrolase HD sub domain
K07814
-
-
0.00000000000001792
78.0
LZS3_k127_7586514_15
PFAM Methyltransferase type 11
-
-
-
0.00000000000002002
82.0
LZS3_k127_7586514_16
Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain
K07658
-
-
0.00000000000006905
77.0
LZS3_k127_7586514_17
Belongs to the bacterial ribosomal protein bS16 family
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp)
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance
Catalyzes the methylthiolation of N6- (dimethylallyl)adenosine (i(6)A), leading to the formation of 2- methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body
K02988
-
-
0.000000000000000000000000000000000000001274
153.0
LZS3_k127_8070772_7
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine
K04075
-
6.3.4.19
0.00000000000000000000000000000000000006563
151.0
LZS3_k127_8070772_8
the 2 termini fold to resemble tRNA(Ala) and it encodes a tag peptide , a short internal open reading frame. During trans-translation Ala- aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA
K03664
-
-
0.0000000000000000000000000000000000001936
145.0
LZS3_k127_8070772_9
The natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
K03043
-
2.7.7.6
0.0
1231.0
LZS3_k127_8610828_1
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
K03046
-
2.7.7.6
0.0
1228.0
LZS3_k127_8610828_10
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr)
ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner
Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A)
amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile)
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and or degradation of damaged proteins
Protein of unknown function (DUF3048) C-terminal domain
-
-
-
0.00000000000000000000000000000000009309
149.0
LZS3_k127_8610828_39
Required for the insertion and or proper folding and or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone
rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation
