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UniProtKB - P76562 (TMCA_ECOLI)

Entry version 145 (02 Jun 2021)
Sequence version 1 (01 Feb 1997)
Previous versions | rss
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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).

UniRule annotation2 Publications

Miscellaneous

Could use an RNA helicase motor driven by ATP hydrolysis to deliver the wobble base of tRNA(Met) to the acetyltransferase domain of TmcA.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.2 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
    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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    • tRNA acetylation Source: EcoCyc
    • tRNA wobble cytosine modification Source: EcoCyc
    Complete GO annotation on QuickGO ...

    <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
    MetaCyc:G7297-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.3.1.193, 2026

    <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)
    <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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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.1 Publication

    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. 1 Publication1
    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

    <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

    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

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		1.20.120.890, 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

    More...    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[»]
    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

    Enzyme and pathway databases

    BioCyciEcoCyc:G7297-MONOMER
    MetaCyc:G7297-MONOMER
    BRENDAi2.3.1.193, 2026

    Miscellaneous databases

    EvolutionaryTraceiP76562

    Protein Ontology

    More...    PROi    		PR:P76562

    Family and domain databases

    Gene3Di1.20.120.890, 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: June 2, 2021
    This is version 145 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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