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
-
-
7.794e-297
935.0
GDHHQS2_k127_1184786_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
-
-
9.674e-230
731.0
GDHHQS2_k127_1184786_10
Belongs to the anti-sigma-factor antagonist family
K04749
-
-
0.00000000000000000000000000006655
119.0
GDHHQS2_k127_1184786_11
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
K01462
-
3.5.1.88
0.000000000000000000000000001424
119.0
GDHHQS2_k127_1184786_12
PFAM peptidase M15B and M15C, D,D-carboxypeptidase VanY endolysin
K07260
-
3.4.17.14
0.000000000000000000000001191
114.0
GDHHQS2_k127_1184786_13
Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase
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)
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)
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
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
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
-
-
0.000000000000000000000000000000000001083
158.0
GDHHQS2_k127_1184786_8
Saccharopine dehydrogenase C-terminal domain
-
-
-
0.00000000000000000000000000000000002199
149.0
GDHHQS2_k127_1184786_9
FAD dependent oxidoreductase
K09471
-
-
0.000000000000000000000000000002401
134.0
GDHHQS2_k127_135618_0
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
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
K02355
-
-
4.589e-265
834.0
GDHHQS2_k127_1483146_1
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis
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
K02933
-
-
0.0000000000000000000000000000000000000000006178
163.0
GDHHQS2_k127_1483146_11
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
K02931
-
-
0.000000000000000000000000000000000000000001567
163.0
GDHHQS2_k127_1483146_12
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs
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
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
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site
K02954
-
-
0.0000000000000000000006009
96.0
GDHHQS2_k127_1483146_29
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 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
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA
K02961
-
-
0.0000000000000000005698
88.0
GDHHQS2_k127_1483146_31
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit
K02895
-
-
0.000000000000000001599
87.0
GDHHQS2_k127_1483146_32
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
K02892
-
-
0.000000000008959
68.0
GDHHQS2_k127_1483146_33
Belongs to the bacterial ribosomal protein bL28 family
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
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
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)
K01870
-
6.1.1.5
2.9e-217
714.0
GDHHQS2_k127_1537843_1
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
This enzyme is involved in nucleotide metabolism it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation
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
K02356
-
-
0.0000000000000000000000000000000001045
139.0
GDHHQS2_k127_1537843_9
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
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)
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves
K06024
-
-
0.000000000000000000000006428
108.0
GDHHQS2_k127_1842992_8
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P)
K01803
-
5.3.1.1
0.000000000000000000000000000000000000000007789
163.0
GDHHQS2_k127_3437270_6
Transposase
-
-
-
0.0000000000000000000000000000001688
132.0
GDHHQS2_k127_3437270_7
Transcriptional regulator, TrmB
-
-
-
0.00000000000000000000000002175
118.0
GDHHQS2_k127_3437270_8
bacterial (prokaryotic) histone like domain
K03530
-
-
0.000000000000000000002412
96.0
GDHHQS2_k127_3437270_9
Belongs to the UPF0102 family
K07460
-
-
0.000000000000000002521
91.0
GDHHQS2_k127_3451825_0
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
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control
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)
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
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)
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
K01358
-
3.4.21.92
0.0000000001783
69.0
GDHHQS2_k127_3546430_15
-
-
-
-
0.0000000005706
65.0
GDHHQS2_k127_3546430_16
Belongs to the bacterial ribosomal protein bL33 family
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 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)
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
-
-
0.000000000000000000000000000000005441
135.0
GDHHQS2_k127_3705524_4
YqeY-like protein
K09117
-
-
0.00000000000000000000000000009257
120.0
GDHHQS2_k127_3705524_5
This protein binds to 23S rRNA in the presence of protein L20
K02888
-
-
0.0000000000000000000002012
101.0
GDHHQS2_k127_3705524_6
6-O-methylguanine DNA methyltransferase, DNA binding domain
K00567,K10778
-
2.1.1.63
0.0000000000000000000004465
97.0
GDHHQS2_k127_3705524_7
DNA binding
-
-
-
0.00003648
51.0
GDHHQS2_k127_400142_0
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
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
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
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
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
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II)
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
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
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
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)
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
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
K01159
-
3.1.22.4
0.00000000000000000000000000001289
126.0
GDHHQS2_k127_4539702_6
Psort location CytoplasmicMembrane, score
K03217
-
-
0.0000000000000000000258
100.0
GDHHQS2_k127_4539702_7
Belongs to the bacterial ribosomal protein bL34 family
K02914
-
-
0.0000000004199
61.0
GDHHQS2_k127_4539702_8
Murein endopeptidase that cleaves the D-alanyl-meso-2,6- diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus
-
-
-
0.0001091
49.0
GDHHQS2_k127_4539702_9
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
Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process
-
-
-
0.00000000000000000000000000000000000000008597
159.0
GDHHQS2_k127_4826313_5
Domain of unknown function (DUF1998)
K06877
-
-
0.00000000000000000000000000001051
126.0
GDHHQS2_k127_4826313_6
Immunoglobulin-like domain of bacterial spore germination
-
-
-
0.0000000000000000008888
93.0
GDHHQS2_k127_4826313_7
phosphatidate phosphatase activity
K19302
-
3.6.1.27
0.0000000000000001468
85.0
GDHHQS2_k127_4990213_0
Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions
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
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors
K02867
-
-
0.0000000000000000000000000000000000000000000969
163.0
GDHHQS2_k127_5011646_2
Protein of unknown function (DUF541)
K09807
-
-
0.0000000000000000000000001147
114.0
GDHHQS2_k127_5011646_3
Haloacid dehalogenase-like hydrolase
K07025
-
-
0.000000178
61.0
GDHHQS2_k127_5011646_4
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation
K03073
-
-
0.00004116
48.0
GDHHQS2_k127_5011646_5
Belongs to the thymidylate synthase family. Archaeal- type ThyA subfamily
K00560
-
2.1.1.45
0.0001927
54.0
GDHHQS2_k127_50724_0
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
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
K00939
-
2.7.4.3
0.00000000005368
70.0
GDHHQS2_k127_50724_12
Belongs to the UPF0235 family
K09131
-
-
0.000000713
53.0
GDHHQS2_k127_50724_13
-
-
-
-
0.00001966
52.0
GDHHQS2_k127_50724_15
Bacterial PH domain
-
-
-
0.00002632
53.0
GDHHQS2_k127_50724_16
Protein of Unknown function (DUF2784)
-
-
-
0.0000355
51.0
GDHHQS2_k127_50724_17
protein conserved in bacteria
-
-
-
0.000047
50.0
GDHHQS2_k127_50724_2
exonuclease of the beta-lactamase fold involved in RNA
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate
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
-
-
0.000000000000000000000000000000002487
133.0
GDHHQS2_k127_50724_7
DoxX
-
-
-
0.000000000000000000000000001303
115.0
GDHHQS2_k127_50724_8
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
K02520
-
-
0.000000000000000000000000008989
116.0
GDHHQS2_k127_50724_9
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
Belongs to the ribulose-phosphate 3-epimerase family
K01783
-
5.1.3.1
0.00000000003036
71.0
GDHHQS2_k127_5324996_0
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
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
K07636
-
2.7.13.3
0.0000000000000000000000000000000000000005534
162.0
GDHHQS2_k127_5324996_11
Cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally Phe) residue
K02654
-
3.4.23.43
0.000000000000000000000000000000000000006488
154.0
GDHHQS2_k127_5324996_12
Type IV pilus assembly protein PilM;
K02662
-
-
0.000000000000000000000000000000008798
141.0
GDHHQS2_k127_5324996_13
Protein of unknown function DUF45
K07043
-
-
0.0000000000000000000000002274
109.0
GDHHQS2_k127_5324996_14
cheY-homologous receiver domain
-
-
-
0.00000000000000000003218
94.0
GDHHQS2_k127_5324996_15
Ribosomal protein S16
K02959
-
-
0.000000000000007134
79.0
GDHHQS2_k127_5324996_17
Belongs to the UPF0109 family
K06960
-
-
0.00000000000009752
75.0
GDHHQS2_k127_5324996_18
cellulase activity
-
-
-
0.0000000000001409
85.0
GDHHQS2_k127_5324996_19
Competence protein
K02242
-
-
0.000000000005975
75.0
GDHHQS2_k127_5324996_2
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)
Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell
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)
K02435
-
6.3.5.6,6.3.5.7
0.0000000002053
68.0
GDHHQS2_k127_5324996_23
cellulose binding
K01179
-
3.2.1.4
0.0000000005475
74.0
GDHHQS2_k127_5324996_24
Fibronectin type 3 domain
-
-
-
0.00000000217
72.0
GDHHQS2_k127_5324996_25
PFAM zinc finger, DksA TraR C4-type
-
-
-
0.000000002913
62.0
GDHHQS2_k127_5324996_26
endopeptidase activity
-
-
-
0.00000001305
68.0
GDHHQS2_k127_5324996_27
PFAM Pentapeptide repeats (8 copies)
-
-
-
0.00000007788
66.0
GDHHQS2_k127_5324996_29
Type IV minor pilin ComP, DNA uptake sequence receptor
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
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)
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
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
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
-
-
0.00000000000000000000001832
111.0
GDHHQS2_k127_6211108_15
-
K07341
-
-
0.00000000000001051
79.0
GDHHQS2_k127_6211108_16
'dna polymerase iii
K02341
-
2.7.7.7
0.00000000001206
74.0
GDHHQS2_k127_6211108_17
Involved in formation and maintenance of cell shape
K03570
-
-
0.0000000411
63.0
GDHHQS2_k127_6211108_18
Belongs to the bacterial ribosomal protein bL32 family
K02911
-
-
0.0003691
48.0
GDHHQS2_k127_6211108_2
Belongs to the class-II aminoacyl-tRNA synthetase family
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
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
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
K02952
-
-
0.00000000000000000000000000000000001438
138.0
GDHHQS2_k127_6553817_13
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit
K02986
-
-
0.00000000000000000000000000000000001638
142.0
GDHHQS2_k127_6553817_14
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
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
-
-
0.0000000000000000000000112
108.0
GDHHQS2_k127_6553817_18
Ribosomal protein L17
K02879
-
-
0.000000000000000000000198
100.0
GDHHQS2_k127_6553817_19
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly
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
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
K02518
-
-
0.0000000000005019
72.0
GDHHQS2_k127_6553817_21
Belongs to the bacterial ribosomal protein bL36 family
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
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
0.00000000000000000000000000001539
126.0
GDHHQS2_k127_6659455_2
Part of the ABC transporter FtsEX involved in cellular division
K09811
-
-
0.0000000000000000000000001984
117.0
GDHHQS2_k127_6659455_4
Immunoglobulin-like domain of bacterial spore germination
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
0.00000000000000000000000000000000009284
139.0
GDHHQS2_k127_6868711_1
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
K10563
-
3.2.2.23,4.2.99.18
0.000000000002906
70.0
GDHHQS2_k127_6868711_2
Binds directly to 16S ribosomal RNA
K02968
-
-
0.00000009747
57.0
GDHHQS2_k127_6894028_0
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
2.207e-247
788.0
GDHHQS2_k127_6894028_1
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
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA
K01489,K07042
-
3.5.4.5
0.00000000002317
69.0
GDHHQS2_k127_7099964_0
Belongs to the class-I aminoacyl-tRNA synthetase family
Belongs to the bacterial ribosomal protein bL27 family
K02899
-
-
0.0000000000000000000001213
99.0
GDHHQS2_k127_7099964_6
binds to the 23S rRNA
K02939
-
-
0.0000000000000000006076
93.0
GDHHQS2_k127_7099964_7
Peptidase, M23
K21471
-
-
0.00000000000000001808
95.0
GDHHQS2_k127_7099964_8
Transglycosylase associated protein
-
-
-
0.00000000000009192
74.0
GDHHQS2_k127_7099964_9
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP)
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
K02357
-
-
0.00000000000000000000000000001342
123.0
GDHHQS2_k127_7286645_0
S4 RNA-binding domain
K06180
-
5.4.99.23
0.000000000000000000000000000000000000000003975
164.0
GDHHQS2_k127_7286645_1
3-ketoacyl-ACP reductase
K00059
-
1.1.1.100
0.0000000000000000000000000000005191
133.0
GDHHQS2_k127_7286645_2
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
K02884
-
-
0.000000000000000000000006566
107.0
GDHHQS2_k127_7286645_3
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation
K01874
-
6.1.1.10
0.00000000000000000000003391
103.0
GDHHQS2_k127_7286645_4
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA
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
