Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 181 (13 Nov 2019)
Sequence version 4 (29 Aug 2003)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Proline--tRNA ligase

Gene

proS

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 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). Misacylated Cys-tRNA(Pro) is not edited by ProRS, but instead may be edited in trans by YbaK.

<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 ‘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=0.25 mM for proline3 Publications
  2. KM=140 mM for alanine3 Publications
  3. KM=0.17 mM for cysteine3 Publications

    <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

    • prolyl-tRNA aminoacylation 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 functionAminoacyl-tRNA synthetase, Ligase
    Biological processProtein biosynthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:PROS-MONOMER
    ECOL316407:JW0190-MONOMER
    MetaCyc:PROS-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    6.1.1.15 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P16659

    <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:
    Proline--tRNA ligase (EC:6.1.1.15)
    Alternative name(s):
    Global RNA synthesis factor
    Prolyl-tRNA synthetase
    Short name:
    ProRS
    <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:proS
    Synonyms:drpA
    Ordered Locus Names:b0194, JW0190
    <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

    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>Mutagenesisi257T → A: Reduces the posttransfer editing activity 5-fold, with little change in both the aminoacylation and the pretransfer editing activities. 1 Publication1
    Mutagenesisi279K → A: Severely affects the posttransfer editing activity, with little change in both the aminoacylation and the pretransfer editing activities. 1 Publication1
    Mutagenesisi350D → A: Abolishes the pretransfer editing activity and reduces the aminoacylation activity 20-fold and the posttransfer editing activity 5-fold. 1 Publication1
    Mutagenesisi369H → A: Reduces both the aminoacylation and the pretransfer editing activities 2.5-fold, and the posttransfer editing activity 5-fold. Loss of specificity in deacylation. 1 Publication1
    Mutagenesisi378D → A: Little change in both the aminoacylation and the editing activities. 1 Publication1
    Mutagenesisi386D → A: Reduces the posttransfer editing activity approximately 2-fold, with little change in both the aminoacylation and the pretransfer editing activities. 1 Publication1
    Mutagenesisi394D → A: Reduces the posttransfer editing activity approximately 2-fold, with little change in both the aminoacylation and the pretransfer editing activities. 1 Publication1
    Mutagenesisi443C → G: 150-fold decrease in posttransfer editing activity against alanine, without change neither in pretransfer editing nor in aminoacylation. 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_00001393291 – 572Proline--tRNA ligaseAdd BLAST572

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P16659

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P16659

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

    More...
    PaxDbi
    P16659

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P16659

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P16659

    PTM databases

    CarbonylDB database of protein carbonylation sites

    More...
    CarbonylDBi
    P16659

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4261629, 32 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10573N

    Protein interaction database and analysis system

    More...
    IntActi
    P16659, 20 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b0194

    <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

    3D structure databases

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

    More...
    SMRi
    P16659

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105C90 Bacteria
    COG0442 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000076893

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P16659

    KEGG Orthology (KO)

    More...
    KOi
    K01881

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P16659

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00779 ProRS_core_prok, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.800, 1 hit
    3.90.960.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01569 Pro_tRNA_synth_type1, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002314 aa-tRNA-synt_IIb
    IPR006195 aa-tRNA-synth_II
    IPR004154 Anticodon-bd
    IPR036621 Anticodon-bd_dom_sf
    IPR002316 Pro-tRNA-ligase_IIa
    IPR004500 Pro-tRNA-synth_IIa_bac-type
    IPR023717 Pro-tRNA-Synthase_IIa_type1
    IPR033730 ProRS_core_prok
    IPR036754 YbaK/aa-tRNA-synt-asso_dom_sf
    IPR007214 YbaK/aa-tRNA-synth-assoc-dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03129 HGTP_anticodon, 1 hit
    PF00587 tRNA-synt_2b, 1 hit
    PF04073 tRNA_edit, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF001535 ProRS_1, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01046 TRNASYNTHPRO

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55826 SSF55826, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00409 proS_fam_II, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50862 AA_TRNA_LIGASE_II, 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.

    P16659-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRTSQYLLST LKETPADAEV ISHQLMLRAG MIRKLASGLY TWLPTGVRVL
    60 70 80 90 100
    KKVENIVREE MNNAGAIEVS MPVVQPADLW QESGRWEQYG PELLRFVDRG
    110 120 130 140 150
    ERPFVLGPTH EEVITDLIRN ELSSYKQLPL NFYQIQTKFR DEVRPRFGVM
    160 170 180 190 200
    RSREFLMKDA YSFHTSQESL QETYDAMYAA YSKIFSRMGL DFRAVQADTG
    210 220 230 240 250
    SIGGSASHEF QVLAQSGEDD VVFSDTSDYA ANIELAEAIA PKEPRAAATQ
    260 270 280 290 300
    EMTLVDTPNA KTIAELVEQF NLPIEKTVKT LLVKAVEGSS FPQVALLVRG
    310 320 330 340 350
    DHELNEVKAE KLPQVASPLT FATEEEIRAV VKAGPGSLGP VNMPIPVVID
    360 370 380 390 400
    RTVAAMSDFA AGANIDGKHY FGINWDRDVA TPEVADIRNV VAGDPSPDGQ
    410 420 430 440 450
    GRLLIKRGIE VGHIFQLGTK YSEALKASVQ GEDGRNQILT MGCYGIGVTR
    460 470 480 490 500
    VVAAAIEQNY DERGIVWPDA IAPFQVAILP MNMHKSFRVQ ELAEKLYSEL
    510 520 530 540 550
    RAQGIEVLLD DRKERPGVMF ADMELIGIPH TIVLGDRNLD NDDIEYKYRR
    560 570
    NGEKQLIKTG DIVEYLVKQI KG
    Length:572
    Mass (Da):63,693
    Last modified:August 29, 2003 - v4
    <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:i312D29390E91C486
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti26 – 27ML → IV (PubMed:2203971).Curated2
    Sequence conflicti127 – 128QL → HV in AAA23710 (PubMed:1688424).Curated2
    Sequence conflicti205 – 216SASHE…VLAQS → RPLTNSRCWRR in AAA23710 (PubMed:1688424).CuratedAdd BLAST12
    Sequence conflicti205S → Q (PubMed:2203971).Curated1
    Sequence conflicti516 – 517PG → RA (PubMed:1688424).Curated2
    Sequence conflicti518 – 572Missing (PubMed:1688424).CuratedAdd BLAST55

    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
    X55518 Genomic DNA Translation: CAA39134.1
    M97858 Genomic DNA Translation: AAA24420.1
    M32357 Genomic DNA Translation: AAA23710.1
    U70214 Genomic DNA Translation: AAB08622.1
    U00096 Genomic DNA Translation: AAC73305.1
    AP009048 Genomic DNA Translation: BAA77870.2
    D15061 Genomic DNA Translation: BAA03654.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B64744 YPEC

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_414736.1, NC_000913.3
    WP_001260717.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC73305; AAC73305; b0194
    BAA77870; BAA77870; BAA77870

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    949116

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW0190
    eco:b0194

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2084

    <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
    X55518 Genomic DNA Translation: CAA39134.1
    M97858 Genomic DNA Translation: AAA24420.1
    M32357 Genomic DNA Translation: AAA23710.1
    U70214 Genomic DNA Translation: AAB08622.1
    U00096 Genomic DNA Translation: AAC73305.1
    AP009048 Genomic DNA Translation: BAA77870.2
    D15061 Genomic DNA Translation: BAA03654.1
    PIRiB64744 YPEC
    RefSeqiNP_414736.1, NC_000913.3
    WP_001260717.1, NZ_LN832404.1

    3D structure databases

    SMRiP16659
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi4261629, 32 interactors
    DIPiDIP-10573N
    IntActiP16659, 20 interactors
    STRINGi511145.b0194

    PTM databases

    CarbonylDBiP16659

    2D gel databases

    SWISS-2DPAGEiP16659

    Proteomic databases

    EPDiP16659
    jPOSTiP16659
    PaxDbiP16659
    PRIDEiP16659

    Genome annotation databases

    EnsemblBacteriaiAAC73305; AAC73305; b0194
    BAA77870; BAA77870; BAA77870
    GeneIDi949116
    KEGGiecj:JW0190
    eco:b0194
    PATRICifig|1411691.4.peg.2084

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0763

    Phylogenomic databases

    eggNOGiENOG4105C90 Bacteria
    COG0442 LUCA
    HOGENOMiHOG000076893
    InParanoidiP16659
    KOiK01881
    PhylomeDBiP16659

    Enzyme and pathway databases

    BioCyciEcoCyc:PROS-MONOMER
    ECOL316407:JW0190-MONOMER
    MetaCyc:PROS-MONOMER
    BRENDAi6.1.1.15 2026
    SABIO-RKiP16659

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P16659

    Family and domain databases

    CDDicd00779 ProRS_core_prok, 1 hit
    Gene3Di3.40.50.800, 1 hit
    3.90.960.10, 1 hit
    HAMAPiMF_01569 Pro_tRNA_synth_type1, 1 hit
    InterProiView protein in InterPro
    IPR002314 aa-tRNA-synt_IIb
    IPR006195 aa-tRNA-synth_II
    IPR004154 Anticodon-bd
    IPR036621 Anticodon-bd_dom_sf
    IPR002316 Pro-tRNA-ligase_IIa
    IPR004500 Pro-tRNA-synth_IIa_bac-type
    IPR023717 Pro-tRNA-Synthase_IIa_type1
    IPR033730 ProRS_core_prok
    IPR036754 YbaK/aa-tRNA-synt-asso_dom_sf
    IPR007214 YbaK/aa-tRNA-synth-assoc-dom
    PfamiView protein in Pfam
    PF03129 HGTP_anticodon, 1 hit
    PF00587 tRNA-synt_2b, 1 hit
    PF04073 tRNA_edit, 1 hit
    PIRSFiPIRSF001535 ProRS_1, 1 hit
    PRINTSiPR01046 TRNASYNTHPRO
    SUPFAMiSSF55826 SSF55826, 1 hit
    TIGRFAMsiTIGR00409 proS_fam_II, 1 hit
    PROSITEiView protein in PROSITE
    PS50862 AA_TRNA_LIGASE_II, 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 nameiSYP_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: P16659
    Secondary accession number(s): P78272, Q59430
    <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: August 1, 1990
    Last sequence update: August 29, 2003
    Last modified: November 13, 2019
    This is version 181 of the entry and version 4 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. SIMILARITY comments
      Index of protein domains and families
    3. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again