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Entry version 148 (25 May 2022)
Sequence version 1 (01 Feb 1997)
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Protein

tRNA(Met) cytidine acetyltransferase TmcA

Gene

tmcA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the formation of N4-acetylcytidine (ac4C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP). It recognizes the wobble base of tRNA(Met), thus distinguishing between tRNA(Met) and the structurally similar tRNA(Ile2) (PubMed:18668122, PubMed:19322199).

Could use an RNA helicase motor driven by ATP hydrolysis to deliver the wobble base of tRNA(Met) to the acetyltransferase domain of TmcA (Probable).

1 Publication2 Publications

Also functions as a lysine 2-hydroxyisobutyryltransferase to regulate transcription. Can specifically catalyze the 2-hydroxyisobutyrylation (Khib) of the DNA-binding protein H-NS. Hydroxyisobutyrylation of H-NS decreases its DNA-binding activity, promotes the expression of acid-resistance genes and enhances bacterial survival under extreme acid stress.

1 Publication

Miscellaneous

467 endogenous Khib candidate sites significantly regulated by TmcA were identified in E.coli using a quantitative proteomics approach.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

ATP/GTP hydrolysis is stimulated by the addition of acetyl-CoA and tRNA(Met). Binding of acetyl-CoA to TmcA activates both ATPase and tRNA-binding activities (PubMed:18668122, PubMed:19322199). ATP promotes the 2-hydroxyisobutyryltransferase activity (PubMed:34903851).3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=2.93 µM for ATP (in the absence of both acetyl-CoA and tRNA(Met))1 Publication
  2. KM=4.16 µM for ATP (in the presence of both acetyl-CoA and tRNA(Met))1 Publication
  3. KM=117 µM for GTP (in the absence of both acetyl-CoA and tRNA(Met))1 Publication
  4. KM=66.6 µM for GTP (in the presence of both acetyl-CoA and tRNA(Met))1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei180ATPUniRule annotation1 Publication1
Binding sitei319ATPUniRule annotation1 Publication1
Binding sitei499Acetyl-CoAUniRule annotation1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei502Important for lysine 2-hydroxyisobutyryltransferase activity1 Publication1
Binding sitei506Acetyl-CoAUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi202 – 211ATPUniRule annotation1 Publication10

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

  • tRNA acetylation Source: EcoCyc
  • tRNA wobble cytosine modification Source: EcoCyc

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, RNA-binding, Transferase, tRNA-binding
Biological processtRNA processing
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G7297-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.1.193, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P76562

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
tRNA(Met) cytidine acetyltransferase TmcAUniRule annotation (EC:2.3.1.193UniRule annotation)
Alternative name(s):
Lysine 2-hydroxyisobutyryltransferase1 Publication (EC:2.3.1.-1 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:tmcAUniRule annotation
Synonyms:ypfI
Ordered Locus Names:b2474, JW2459
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutants lack the ac4C modification, but do not show any growth defects (PubMed:18668122). Knockout mutant shows decreased 2-hydroxyisobutyrylation levels (PubMed:34903851).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi287T → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication1
Mutagenesisi291Y → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication1
Mutagenesisi292E → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication1
Mutagenesisi296R → A: Decrease in ATPase activity and loss of tRNA-binding. 1 Publication1
Mutagenesisi301K → A: Decrease in ATPase activity and loss of tRNA-binding. 1 Publication1
Mutagenesisi319R → A: Loss of ATPase activity, but no change in tRNA-binding. Lack of hydroxyisobutyrylation activity. 2 Publications1
Mutagenesisi327E → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication1
Mutagenesisi377H → A: Decrease in ATPase activity and loss of tRNA-binding. 1 Publication1
Mutagenesisi387R → A: Abolishes the tRNA-binding capacity, but no loss of activity. 1 Publication1
Mutagenesisi460R → A: Loss of tRNA-binding. 1 Publication1
Mutagenesisi463V → A: Does not affect hydroxyisobutyrylation activity. 1 Publication1
Mutagenesisi469R → A: Does not affect hydroxyisobutyrylation activity. 1 Publication1
Mutagenesisi471G → A: Does not affect hydroxyisobutyrylation activity. 1 Publication1
Mutagenesisi502R → A: Lack of hydroxyisobutyrylation activity. Has little effect on RNA acetylation activity. Alters binding with hydroxyisobutanoyl-CoA, but not with acetyl-CoA. 1 Publication1
Mutagenesisi504W → A: Does not affect hydroxyisobutyrylation activity. No change in acetyl-CoA or hydroxyisobutanoyl-CoA binding. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001692391 – 671tRNA(Met) cytidine acetyltransferase TmcAAdd BLAST671

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P76562

PRoteomics IDEntifications database

More...
PRIDEi
P76562

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4259195, 20 interactors

Database of interacting proteins

More...
DIPi
DIP-12825N

Protein interaction database and analysis system

More...
IntActi
P76562, 8 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2474

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1671
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P76562

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P76562

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P76562

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini356 – 531N-acetyltransferaseUniRule annotationAdd BLAST176

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni461 – 463Acetyl-CoA bindingUniRule annotation1 Publication3
Regioni468 – 474Acetyl-CoA bindingUniRule annotation1 Publication7

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RNA cytidine acetyltransferase family. TmcA subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1444, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_004652_1_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P76562

Identification of Orthologs from Complete Genome Data

More...
OMAi
NEPDDLG

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P76562

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.120.890, 1 hit
3.40.50.300, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01886, tRNA_acetyltr_TmcA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016181, Acyl_CoA_acyltransferase
IPR000182, GNAT_dom
IPR007807, Helicase_dom
IPR027417, P-loop_NTPase
IPR032672, TmcA/NAT10/Kre33
IPR038321, TmcA_C_sf
IPR013562, TmcA_N
IPR033442, TmcA_tRNA_bind
IPR024914, tRNA_acetyltr_TmcA

The PANTHER Classification System

More...
PANTHERi
PTHR10925, PTHR10925, 2 hits

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08351, DUF1726, 1 hit
PF13718, GNAT_acetyltr_2, 1 hit
PF05127, Helicase_RecD, 1 hit
PF17176, tRNA_bind_3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 1 hit
SSF55729, SSF55729, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51186, GNAT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P76562-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAELTALHTL TAQMKREGIR RLLVLSGEEG WCFEHTLKLR DALPGDWLWI
60 70 80 90 100
SPRPDAENHC SPSALQTLLG REFRHAVFDA RHGFDAAAFA ALSGTLKAGS
110 120 130 140 150
WLVLLLPVWE EWENQPDADS LRWSDCPDPI ATPHFVQHLK RVLTADNEAI
160 170 180 190 200
LWRQNQPFSL AHFTPRTDWY PATGAPQPEQ QQLLKQLMTM PPGVAAVTAA
210 220 230 240 250
RGRGKSALAG QLISRIAGRA IVTAPAKAST DVLAQFAGEK FRFIAPDALL
260 270 280 290 300
ASDEQADWLV VDEAAAIPAP LLHQLVSRFP RTLLTTTVQG YEGTGRGFLL
310 320 330 340 350
KFCARFPHLH RFELQQPIRW AQGCPLEKMV SEALVFDDEN FTHTPQGNIV
360 370 380 390 400
ISAFEQTLWQ SDPETPLKVY QLLSGAHYRT SPLDLRRMMD APGQHFLQAA
410 420 430 440 450
GENEIAGALW LVDEGGLSQQ LSQAVWAGFR RPRGNLVAQS LAAHGNNPLA
460 470 480 490 500
ATLRGRRVSR IAVHPARQRE GTGRQLIAGA LQYTQDLDYL SVSFGYTGEL
510 520 530 540 550
WRFWQRCGFV LVRMGNHREA SSGCYTAMAL LPMSDAGKQL AEREHYRLRR
560 570 580 590 600
DAQALAQWNG ETLPVDPLND AVLSDDDWLE LAGFAFAHRP LLTSLGCLLR
610 620 630 640 650
LLQTSELALP ALRGRLQKNA SDAQLCTTLK LSGRKMLLVR QREEAAQALF
660 670
ALNDVRTERL RDRITQWQLF H
Length:671
Mass (Da):74,893
Last modified:February 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i07C5A019570CDA5D
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC75527.1
AP009048 Genomic DNA Translation: BAA16352.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A65023

NCBI Reference Sequences

More...
RefSeqi
NP_416969.1, NC_000913.3
WP_000829360.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75527; AAC75527; b2474
BAA16352; BAA16352; BAA16352

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946053

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2459
eco:b2474

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4265

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC75527.1
AP009048 Genomic DNA Translation: BAA16352.2
PIRiA65023
RefSeqiNP_416969.1, NC_000913.3
WP_000829360.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZPAX-ray2.35A/B1-671[»]
AlphaFoldDBiP76562
SMRiP76562
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259195, 20 interactors
DIPiDIP-12825N
IntActiP76562, 8 interactors
STRINGi511145.b2474

Proteomic databases

PaxDbiP76562
PRIDEiP76562

Genome annotation databases

EnsemblBacteriaiAAC75527; AAC75527; b2474
BAA16352; BAA16352; BAA16352
GeneIDi946053
KEGGiecj:JW2459
eco:b2474
PATRICifig|1411691.4.peg.4265

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB3948

Phylogenomic databases

eggNOGiCOG1444, Bacteria
HOGENOMiCLU_004652_1_1_6
InParanoidiP76562
OMAiNEPDDLG
PhylomeDBiP76562

Enzyme and pathway databases

BioCyciEcoCyc:G7297-MONOMER
BRENDAi2.3.1.193, 2026
SABIO-RKiP76562

Miscellaneous databases

EvolutionaryTraceiP76562

Protein Ontology

More...
PROi
PR:P76562

Family and domain databases

Gene3Di1.20.120.890, 1 hit
3.40.50.300, 1 hit
HAMAPiMF_01886, tRNA_acetyltr_TmcA, 1 hit
InterProiView protein in InterPro
IPR016181, Acyl_CoA_acyltransferase
IPR000182, GNAT_dom
IPR007807, Helicase_dom
IPR027417, P-loop_NTPase
IPR032672, TmcA/NAT10/Kre33
IPR038321, TmcA_C_sf
IPR013562, TmcA_N
IPR033442, TmcA_tRNA_bind
IPR024914, tRNA_acetyltr_TmcA
PANTHERiPTHR10925, PTHR10925, 2 hits
PfamiView protein in Pfam
PF08351, DUF1726, 1 hit
PF13718, GNAT_acetyltr_2, 1 hit
PF05127, Helicase_RecD, 1 hit
PF17176, tRNA_bind_3, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
SSF55729, SSF55729, 1 hit
PROSITEiView protein in PROSITE
PS51186, GNAT, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTMCA_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P76562
Secondary accession number(s): P76972
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 25, 2022
This is version 148 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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