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Entry version 83 (02 Jun 2021)
Sequence version 1 (21 Mar 2006)
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Protein

Sortase A

Gene

srtA

Organism
Staphylococcus aureus (strain NCTC 8325 / PS 47)
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

Transpeptidase that anchors surface proteins to the cell wall (PubMed:10427003, PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224).

Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224).

This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224).

Utilizes lipid II as the peptidoglycan substrate for the sorting reaction (PubMed:10446208, PubMed:11856734).

Responsible for the display of important virulence factors (PubMed:14769030).

Important for interactions with the host and host colonization during infection (PubMed:10805806, PubMed:14769030).

8 Publications

<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

Sortase activity is regulated by monomer-homodimer equilibrium. Mutant cells with monomeric SrtA display more adhesive proteins on the cell surface and are more invasive than wild-type cells, which have majority of SrtA in dimeric form. Dimerization may suppress the enzymatic activity on cell membranes (PubMed:26129884). Stimulated by calcium ions, which promote substrate binding (PubMed:11371637, PubMed:16269411). Calcium ions bind to SrtA and modulate both the structure and dynamics of a large active site loop (PubMed:16269411). Can also be stimulated, to a lesser extent, by Mg2+ and Mn2+ (PubMed:11371637). Inhibited by sulfhydryl-modifying reagents (PubMed:10535938, PubMed:10446208).5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi105Calcium1 Publication1 Publication1
Metal bindingi108Calcium1 Publication1 Publication1
Metal bindingi112Calcium1 Publication1 Publication1
Metal bindingi114Calcium1 Publication1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei120Proton donor/acceptor5 Publications1
Metal bindingi171Calcium1 Publication1 Publication1
Active sitei184Acyl-thioester intermediate5 Publications1
<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>Sitei197Transition state stabilizer3 Publications1

<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

<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 functionHydrolase, Protease, Thiol protease
LigandMetal-binding

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C60.001

<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:
Sortase ACurated (EC:3.4.22.707 Publications)
Alternative name(s):
Surface protein sorting A1 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:srtA1 Publication
Ordered Locus Names:SAOUHSC_02834Imported
<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>OrganismiStaphylococcus aureus (strain NCTC 8325 / PS 47)
<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 identifieri93061 [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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
<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
  • UP000008816 <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

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 6Cytoplasmic1 Publication6
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei7 – 24Helical; Note=Membrane anchorSequence analysis1 PublicationAdd BLAST18
Topological domaini25 – 206Extracellular1 PublicationAdd BLAST182

Keywords - Cellular componenti

Cell membrane, Membrane

<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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Could be used as a target for the development of antivirulence chemotherapeutics against Gram-positive bacterial pathogens.1 Publication

<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 fail to cleave and anchor surface proteins (PubMed:10427003, PubMed:10805806). Protein secretion pathway is not affected (PubMed:10805806). Mutants are defective in the establishment of animal infections (PubMed:10805806).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>Mutagenesisi97L → A: Decrease in activity. 1 Publication1
Mutagenesisi98N → A or Q: No change in sortase activity. 1 Publication1
Mutagenesisi104A → G: Decrease in activity. 1 Publication1
Mutagenesisi108E → A: Retains enzymatic activity. Shows reduced Ca(2+) sensitivity. 1 Publication1
Mutagenesisi118A → G: Decrease in activity. 1 Publication1
Mutagenesisi120H → A: Almost loss or loss of activity. 2 Publications1
Mutagenesisi120H → Q: Almost loss of activity. 1 Publication1
Mutagenesisi132N → A: Does not affect dimerization of the full-length protein. Disrupts dimerization; when associated with A-137 and A-143. 1 Publication1
Mutagenesisi137K → A: Does not affect dimerization of the full-length protein. Disrupts dimerization; when associated with A-132 and A-143. 1 Publication1
Mutagenesisi143Y → A: Does not affect dimerization of the full-length protein. Disrupts dimerization; when associated with A-132 and A-137. 1 Publication1
Mutagenesisi170D → A: Retains enzymatic activity. No change in dependence on Ca(2+). 1 Publication1
Mutagenesisi171E → A: Retains enzymatic activity. Shows reduced Ca(2+) sensitivity. 1 Publication1
Mutagenesisi180T → A: Decrease in catalytic efficiency. 1 Publication1
Mutagenesisi181L → A: Decrease in catalytic efficiency. 1 Publication1
Mutagenesisi182I → A or S: Decrease in catalytic efficiency. 1 Publication1
Mutagenesisi183T → A: Strong decrease in catalytic efficiency. 1 Publication1
Mutagenesisi184C → A: Abolishes sortase activity. 3 Publications1
Mutagenesisi184C → H: Loss of activity. 1 Publication1
Mutagenesisi184C → R: Abolishes sortase processing; when associated with C-197. 1 Publication1
Mutagenesisi184C → S: Retains low levels of activity. 1 Publication1
Mutagenesisi185D → A: No change in activity. 1 Publication1
Mutagenesisi186D → A: No change in activity. 1 Publication1
Mutagenesisi194W → A: Decreases the transpeptidase activity. 1 Publication1
Mutagenesisi197R → A or K: Strong decrease in catalytic efficiency. Does not affect substrate cleavage specificity. Severe decrease in sortase transpeptidase activity. 2 Publications1
Mutagenesisi197R → C: Abolishes sortase processing; when associated with R-184. 1 Publication1
Mutagenesisi197R → H: Does not affect substrate cleavage specificity. Severe decrease in sortase transpeptidase activity. 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_00004452681 – 206Sortase AAdd BLAST206

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer and homodimer; in equilibrium.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
1280.SAXN108_2777

<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

1206
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
Q2FV99

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

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SMRi
Q2FV99

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

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>Regioni49 – 69DisorderedSequence analysisAdd BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi49 – 65Basic and acidic residuesSequence analysisAdd BLAST17

<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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG3764, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_1405331_0_0_9

Identification of Orthologs from Complete Genome Data

More...
OMAi
MRADQKM

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06165, Sortase_A, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.260.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005754, Sortase
IPR042007, Sortase_A
IPR023365, Sortase_dom-sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04203, Sortase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF63817, SSF63817, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01076, sortase_fam, 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.

Q2FV99-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKWTNRLMT IAGVVLILVA AYLFAKPHID NYLHDKDKDE KIEQYDKNVK
60 70 80 90 100
EQASKDKKQQ AKPQIPKDKS KVAGYIEIPD ADIKEPVYPG PATPEQLNRG
110 120 130 140 150
VSFAEENESL DDQNISIAGH TFIDRPNYQF TNLKAAKKGS MVYFKVGNET
160 170 180 190 200
RKYKMTSIRD VKPTDVGVLD EQKGKDKQLT LITCDDYNEK TGVWEKRKIF

VATEVK
Length:206
Mass (Da):23,541
Last modified:March 21, 2006 - 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:iDC3E65C51E145C7B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CP000253 Genomic DNA Translation: ABD31836.1

NCBI Reference Sequences

More...
RefSeqi
WP_000759361.1, NZ_LS483365.1
YP_501293.1, NC_007795.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABD31836; ABD31836; SAOUHSC_02834

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3921273

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sao:SAOUHSC_02834

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|93061.5.peg.2564

<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
CP000253 Genomic DNA Translation: ABD31836.1
RefSeqiWP_000759361.1, NZ_LS483365.1
YP_501293.1, NC_007795.1

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
1IJANMR-A59-206[»]
1T2OX-ray2.30A/B/C61-206[»]
1T2PX-ray2.00A/B/C61-206[»]
1T2WX-ray1.80A/B/C62-206[»]
2KIDNMR-A59-206[»]
6R1VNMR-A59-206[»]
BMRBiQ2FV99
SMRiQ2FV99
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi1280.SAXN108_2777

Protein family/group databases

MEROPSiC60.001

Genome annotation databases

EnsemblBacteriaiABD31836; ABD31836; SAOUHSC_02834
GeneIDi3921273
KEGGisao:SAOUHSC_02834
PATRICifig|93061.5.peg.2564

Phylogenomic databases

eggNOGiCOG3764, Bacteria
HOGENOMiCLU_1405331_0_0_9
OMAiMRADQKM

Family and domain databases

CDDicd06165, Sortase_A, 1 hit
Gene3Di2.40.260.10, 1 hit
InterProiView protein in InterPro
IPR005754, Sortase
IPR042007, Sortase_A
IPR023365, Sortase_dom-sf
PfamiView protein in Pfam
PF04203, Sortase, 1 hit
SUPFAMiSSF63817, SSF63817, 1 hit
TIGRFAMsiTIGR01076, sortase_fam, 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 nameiSRTA_STAA8
<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: Q2FV99
<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: October 10, 2018
Last sequence update: March 21, 2006
Last modified: June 2, 2021
This is version 83 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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