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Entry version 137 (11 Dec 2019)
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).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_section">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_section">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_section">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_section">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
    ECOL316407:JW2459-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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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

    GO - Cellular componenti

    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_and_biotech_section">'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.<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_and_domains_section">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
    ENOG4105E0I Bacteria
    COG1444 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000283762

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P76562

    KEGG Orthology (KO)

    More...
    KOi
    K06957

    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, 1 hit
    PTHR10925:SF6 PTHR10925:SF6, 1 hit

    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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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

    eggNOGiENOG4105E0I Bacteria
    COG1444 LUCA
    HOGENOMiHOG000283762
    InParanoidiP76562
    KOiK06957

    Enzyme and pathway databases

    BioCyciEcoCyc:G7297-MONOMER
    ECOL316407:JW2459-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, 1 hit
    PTHR10925:SF6 PTHR10925:SF6, 1 hit
    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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_and_isoforms">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: December 11, 2019
    This is version 137 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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