Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane
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)
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
Belongs to the bacterial ribosomal protein bL32 family
K02911
GO:0003674,GO:0003735,GO:0005198
-
0.00000008907
55.0
SRR21617311_k127_1979009_16
Carrier of the growing fatty acid chain in fatty acid biosynthesis
K02078
-
-
0.000001489
54.0
SRR21617311_k127_1979009_17
Belongs to the UPF0109 family
K06960
-
-
0.00001868
49.0
SRR21617311_k127_1979009_18
Prokaryotic N-terminal methylation motif
K02456
-
-
0.00004862
52.0
SRR21617311_k127_1979009_19
Type II transport protein GspH
K02457
-
-
0.00006981
52.0
SRR21617311_k127_1979009_2
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
Cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally Phe) residue
K02654
-
3.4.23.43
0.000000000000000000000000000000000000003248
156.0
SRR21617311_k127_1979009_5
TIGRFAM type IV pilus assembly protein PilM
K02662
-
-
0.0000000000000000000000000000000004909
143.0
SRR21617311_k127_1979009_6
Radical SAM domain protein
K06139
-
-
0.000000000000000000000000000001472
136.0
SRR21617311_k127_1979009_7
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
-
-
0.00000000000000000005268
93.0
SRR21617311_k127_1979009_8
Ribosomal protein S16
K02959
-
-
0.000000000000004226
78.0
SRR21617311_k127_1979009_9
NUDIX domain
-
-
-
0.0000000000004474
75.0
SRR21617311_k127_2011390_0
Participates in initiation and elongation during chromosome replication
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA
K03438
-
2.1.1.199
0.0000000000000000000000002959
110.0
SRR21617311_k127_2020784_3
Belongs to the MraZ family
K03925
-
-
0.0000000000000000000001868
102.0
SRR21617311_k127_2100420_0
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
1095.0
SRR21617311_k127_2100420_1
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate
K01007
-
2.7.9.2
9.327e-226
722.0
SRR21617311_k127_2100420_10
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
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
PFAM Bacterial extracellular solute-binding proteins, family 5 Middle
K02035
-
-
0.00000000000000000000000000000000003048
150.0
SRR21617311_k127_2100420_16
Inositol monophosphatase
K01092
-
3.1.3.25
0.0000000000000000000000000000000006371
140.0
SRR21617311_k127_2100420_17
Psort location CytoplasmicMembrane, score
-
-
-
0.00000000000000000000002033
116.0
SRR21617311_k127_2100420_19
excinuclease ABC
-
-
-
0.0000000000000006435
80.0
SRR21617311_k127_2100420_2
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
-
-
1.34e-223
711.0
SRR21617311_k127_2100420_20
Evidence 5 No homology to any previously reported sequences
K09005
-
-
0.0000000000001019
79.0
SRR21617311_k127_2100420_21
Transglutaminase-like superfamily
-
-
-
0.0000000000001314
84.0
SRR21617311_k127_2100420_22
serine-type peptidase activity
-
-
-
0.000000000192
67.0
SRR21617311_k127_2100420_23
PFAM Bacterial regulatory protein, arsR family
K21903
-
-
0.000000002832
63.0
SRR21617311_k127_2100420_24
-
-
-
-
0.000002602
49.0
SRR21617311_k127_2100420_25
Mycobacterial 4 TMS phage holin, superfamily IV
K08972
-
-
0.00001009
55.0
SRR21617311_k127_2100420_26
Belongs to the glycosyl hydrolase 5 (cellulase A) family
-
-
-
0.00001126
57.0
SRR21617311_k127_2100420_27
-
-
-
-
0.00001449
54.0
SRR21617311_k127_2100420_28
cell wall organization
-
-
-
0.00003138
53.0
SRR21617311_k127_2100420_29
Preprotein translocase SecG subunit
K03075
-
-
0.0000551
49.0
SRR21617311_k127_2100420_3
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate
TIGRFAM cell envelope-related function transcriptional attenuator
-
-
-
0.0001455
52.0
SRR21617311_k127_2100420_4
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
Catalyzes the reversible conversion of 2- phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII
Catalyzes the decarboxylative condensation of pimeloyl- acyl-carrier protein and L-alanine to produce 8-amino-7- oxononanoate (AON), acyl-carrier protein , and carbon dioxide
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
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
-
-
0.0000000000000000000000000000000000000000000259
167.0
SRR21617311_k127_2119899_8
decarboxylase
K01585
-
4.1.1.19
0.000000000000000000000000000000000004968
154.0
SRR21617311_k127_2119899_9
Bacteriocin-protection, YdeI or OmpD-Associated
-
-
-
0.00000000000000000000000000000003839
126.0
SRR21617311_k127_2274423_0
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family
Immunoglobulin-like domain of bacterial spore germination
-
-
-
0.0000000005194
69.0
SRR21617311_k127_2274423_9
COG0741 Soluble lytic murein transglycosylase and related regulatory proteins (some contain LysM invasin domains)
K08309
-
-
0.000000001062
68.0
SRR21617311_k127_2289899_0
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
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
-
-
0.000000000000000000000009912
107.0
SRR21617311_k127_2289899_15
Reverse transcriptase-like
K03469,K06864
-
3.1.26.4
0.0000000000000000000001303
103.0
SRR21617311_k127_2289899_16
von Willebrand factor, type A
-
-
-
0.0000000000000000000007134
106.0
SRR21617311_k127_2289899_17
Could be involved in insertion of integral membrane proteins into the membrane
K03424,K08998
-
-
0.00000000000000000022
89.0
SRR21617311_k127_2289899_18
Psort location Cytoplasmic, score
-
-
-
0.00000000000000008499
87.0
SRR21617311_k127_2289899_19
Belongs to the NUDIX hydrolase family
-
-
-
0.000000000005629
73.0
SRR21617311_k127_2289899_2
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
Belongs to the bacterial ribosomal protein bL34 family
K02914
-
-
0.0000000004529
62.0
SRR21617311_k127_2289899_23
multi-organism process
-
-
-
0.0000000007425
68.0
SRR21617311_k127_2289899_24
PFAM Stage II sporulation D domain protein
-
-
-
0.00000001274
68.0
SRR21617311_k127_2289899_25
protein serine/threonine phosphatase activity
-
-
-
0.00000006094
66.0
SRR21617311_k127_2289899_26
COG0494 NTP pyrophosphohydrolases including oxidative damage repair enzymes
-
-
-
0.00000468
54.0
SRR21617311_k127_2289899_27
PFAM membrane-flanked domain
-
-
-
0.00001787
54.0
SRR21617311_k127_2289899_28
-O-antigen
K02847
-
-
0.00002524
56.0
SRR21617311_k127_2289899_29
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
DnaJ-class molecular chaperone with C-terminal Zn finger domain
-
-
-
0.00008004
54.0
SRR21617311_k127_2289899_31
FR47-like protein
K00657
-
2.3.1.57
0.00009791
50.0
SRR21617311_k127_2289899_32
UDP-4-amino-4-deoxy-L-arabinose aminotransferase
K13010
-
2.6.1.102
0.000164
49.0
SRR21617311_k127_2289899_33
-
-
-
-
0.0003761
47.0
SRR21617311_k127_2289899_34
heat shock protein binding
K03686
-
-
0.0007487
49.0
SRR21617311_k127_2289899_4
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
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
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)
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
0.000000000000003859
80.0
SRR21617311_k127_2488330_16
Glycosyl hydrolase
-
-
-
0.0000000000002137
77.0
SRR21617311_k127_2488330_17
Bacterial Ig-like domain (group 3)
K20276
-
-
0.00000000002792
73.0
SRR21617311_k127_2488330_2
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)
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
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)
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)
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
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
K02887
-
-
0.0000000000000000000000000004455
116.0
SRR21617311_k127_2709614_9
Belongs to the bacterial ribosomal protein bL35 family
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme
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
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
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
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)
DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N- glycosidic bond, leaving an AP (apurinic apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
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
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
-
-
0.0000000000000000000000000000000000000001261
153.0
SRR21617311_k127_2777705_25
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body
K02988
-
-
0.0000000000000000000000000000000000000008819
153.0
SRR21617311_k127_2777705_26
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
K02871
-
-
0.000000000000000000000000000000000000001707
151.0
SRR21617311_k127_2777705_27
Protein of unknown function (DUF3048) C-terminal domain
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
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome
K02874
-
-
0.00000000000000000000000000000000012
136.0
SRR21617311_k127_2777705_33
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
-
-
0.0000000000000000000000000000000004021
135.0
SRR21617311_k127_2777705_34
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
0.00000000000000000000000000000000422
136.0
SRR21617311_k127_2777705_35
nuclease
-
-
-
0.000000000000000000000000000000006005
137.0
SRR21617311_k127_2777705_36
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA
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 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
-
-
0.0000000000000000000002164
97.0
SRR21617311_k127_2777705_42
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
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
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
-
-
0.000000008468
60.0
SRR21617311_k127_2777705_59
Binds to the 23S rRNA
K02876
-
-
0.0003284
46.0
SRR21617311_k127_2777705_6
ATPase, P-type (transporting), HAD superfamily, subfamily IC
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
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
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
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
-
-
1.63e-270
859.0
SRR21617311_k127_2798379_1
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner
Metal dependent phosphohydrolases with conserved 'HD' motif.
K06951
-
-
0.000000000000000000000000000000000000000001186
163.0
SRR21617311_k127_2798379_15
G T U mismatch-specific DNA glycosylase
-
-
-
0.00000000000000000000000000000000001052
141.0
SRR21617311_k127_2798379_16
HD domain
K07023
-
-
0.00000000000000000000000000000000104
137.0
SRR21617311_k127_2798379_17
Pyridoxamine 5'-phosphate oxidase
-
-
-
0.0000000000000000000000000000001022
128.0
SRR21617311_k127_2798379_18
NUDIX domain
K01515
-
3.6.1.13
0.0000000000000000000000000000003544
128.0
SRR21617311_k127_2798379_19
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
-
-
0.000000000000000000000000000001136
128.0
SRR21617311_k127_2798379_2
Belongs to the class-II aminoacyl-tRNA synthetase family
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA RNA and avoiding chromosomal lesions
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
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp Asn)
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)
DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function
Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)- butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP MEP pathway for isoprenoid precursor biosynthesis
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
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
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation
K02935
-
-
0.00000000003061
69.0
SRR21617311_k127_2937139_31
RimK domain protein ATP-grasp
K05844
-
-
0.000000001647
68.0
SRR21617311_k127_2937139_32
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation
Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force
K15987
-
3.6.1.1
1.819e-241
764.0
SRR21617311_k127_313085_1
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
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
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
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
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome
K02956
-
-
0.000000000000000000000001825
107.0
SRR21617311_k127_323642_18
Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane
K03980
-
-
0.00000000000000000000002645
111.0
SRR21617311_k127_323642_19
serine-type endopeptidase activity
K04771
-
3.4.21.107
0.0000000000000000002013
104.0
SRR21617311_k127_323642_2
Hsp70 protein
K04043
-
-
2.997e-228
723.0
SRR21617311_k127_323642_20
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA
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
-
-
0.0000000009337
66.0
SRR21617311_k127_323642_23
TIGRFAM phosphodiesterase, MJ0936 family
K07095
-
-
0.00000001819
61.0
SRR21617311_k127_323642_24
cellulase activity
-
-
-
0.000002547
58.0
SRR21617311_k127_323642_25
Domain of unknown function (DUF4115)
K15539
-
-
0.00005887
53.0
SRR21617311_k127_323642_26
tRNA nucleotidyltransferase poly(A) polymerase
K00974
-
2.7.7.72
0.0001715
53.0
SRR21617311_k127_323642_3
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction
K00962
-
2.7.7.8
1.476e-199
646.0
SRR21617311_k127_323642_4
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
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. 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
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner
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 reduction of dTDP-6-deoxy-L-lyxo-4- hexulose to yield dTDP-L-rhamnose
K00067
-
1.1.1.133
0.000000000000000000000000000000001941
140.0
SRR21617311_k127_608954_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
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source
K00820
-
2.6.1.16
2.366e-201
644.0
SRR21617311_k127_692141_1
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
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
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P)
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
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
3-methyladenine DNA glycosylase 8-oxoguanine DNA glycosylase
-
-
-
0.000000000000000000000000000000000000002826
158.0
SRR21617311_k127_692141_25
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
-
-
0.0000000000000000000000000000000000006022
145.0
SRR21617311_k127_692141_26
Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides
K02759,K03478
-
2.7.1.196,2.7.1.205,3.5.1.105
0.000000000000000000000000000000000002862
146.0
SRR21617311_k127_692141_27
Psort location Cytoplasmic, score
K02503
-
-
0.00000000000000000000000000000001144
130.0
SRR21617311_k127_692141_28
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
-
-
0.000000000000000000000000000001172
126.0
SRR21617311_k127_692141_29
HlyD family secretion protein
K02005,K13888
-
-
0.00000000000000000000000000002279
131.0
SRR21617311_k127_692141_3
TIGRFAM cell shape determining protein, MreB Mrl family
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
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis
K00943
-
2.7.4.9
0.00000000000000000000000003617
116.0
SRR21617311_k127_692141_32
Yqey-like protein
K09117
-
-
0.000000000000000000000004114
107.0
SRR21617311_k127_692141_33
Thymidylate kinase
K15518
-
2.7.1.113
0.0000000000000000000023
102.0
SRR21617311_k127_692141_34
Belongs to the D-alanine--D-alanine ligase family
K01921
-
6.3.2.4
0.00000000000000000001494
104.0
SRR21617311_k127_692141_35
GHMP kinases C terminal
-
-
-
0.0000000000000000009785
97.0
SRR21617311_k127_692141_36
Catalyzes the ADP transfer from ATP to D-glycero-beta-D- manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno- heptose
K03272
-
2.7.1.167,2.7.7.70
0.000000000000000004177
89.0
SRR21617311_k127_692141_37
Formiminotransferase-cyclodeaminase
-
-
-
0.00000000000000001483
88.0
SRR21617311_k127_692141_38
PFAM NUDIX hydrolase
-
-
-
0.00000000000000007327
87.0
SRR21617311_k127_692141_39
Metallo-beta-lactamase superfamily
K03801,K06167
-
2.3.1.181,3.1.4.55
0.000000000000004788
83.0
SRR21617311_k127_692141_4
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
Belongs to the bacterial ribosomal protein bL33 family
K02913
-
-
0.00000001294
62.0
SRR21617311_k127_692141_51
Haloacid dehalogenase-like hydrolase
K07025
-
-
0.00000001503
62.0
SRR21617311_k127_692141_52
NUDIX domain
K03574
-
3.6.1.55
0.00000004086
60.0
SRR21617311_k127_692141_53
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA
Belongs to the bacterial ribosomal protein bL28 family
K02902
GO:0003674,GO:0003735,GO:0005198
-
0.000000578
54.0
SRR21617311_k127_692141_55
AAA domain
K07028
-
-
0.0000009869
57.0
SRR21617311_k127_692141_56
PFAM peptidase S1 and S6, chymotrypsin Hap
K04771,K04772
-
3.4.21.107
0.000001487
57.0
SRR21617311_k127_692141_57
-
-
-
-
0.000002722
53.0
SRR21617311_k127_692141_59
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis
K01489
-
3.5.4.5
0.00001399
57.0
SRR21617311_k127_692141_6
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 NADPH and FADH(2) as the reductant
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
0.00000000000000000000000000000002335
131.0
SRR21617311_k127_721471_4
-
-
-
-
0.00000000000000000000001685
104.0
SRR21617311_k127_721471_5
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 reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and or for immediate growth after restoration of oxygen
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
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
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
Belongs to the 'phage' integrase family. XerC subfamily
K03733,K04763
-
-
0.000000000000000000000000001082
123.0
SRR21617311_k127_946942_43
The natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis
K01056
-
3.1.1.29
0.000000000000000000000000001412
117.0
SRR21617311_k127_946942_44
dephospho-CoA kinase activity
-
-
-
0.00000000000000000000000001048
117.0
SRR21617311_k127_946942_46
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation