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UniProtKB - P0A7B8 (HSLV_ECOLI)

Entry version 141 (23 Feb 2022)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
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Protein

ATP-dependent protease subunit HslV

Gene

hslV

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

Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.

UniRule annotation7 Publications

Caution

PubMed:9013898 sequence is supposed to originate from rat but, based on sequence similarity, it seems that this is a case of bacterial contamination from E.coli.Curated

<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

Allosterically activated by HslU binding.Curated

<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

Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.
  1. KM=5.2 µM for Arc-MYL-st11 (at 37 degrees Celsius)1 Publication

Temperature dependencei

Optimum temperature is 55 degrees Celsius.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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei2UniRule annotation1 Publication1
<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 bindingi157Sodium; via carbonyl oxygen1
Metal bindingi160Sodium; via carbonyl oxygen1
Metal bindingi163Sodium; via carbonyl oxygen1

<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

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 functionAllosteric enzyme, Hydrolase, Protease, Threonine protease
Biological processStress response
LigandMetal-binding, Sodium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG11676-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.25.2, 2026

Protein family/group databases

MEROPS protease database

More...MEROPSi		T01.006

<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:
ATP-dependent protease subunit HslVUniRule annotation (EC:3.4.25.2UniRule annotation)
Alternative name(s):
Heat shock protein HslVUniRule 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:hslVUniRule annotation
Synonyms:htpO, yiiC
Ordered Locus Names:b3932, JW3903
<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

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>Mutagenesisi2T → S: 80% reduced protease activity in the absence of HslU. Almost no effect in the presence of HslU. 1 Publication1
Mutagenesisi2T → V: No protease activity. 1 Publication1
Mutagenesisi3T → S or V: 80% reduced protease activity. 1 Publication1
Mutagenesisi6S → A: No effect. 1 Publication1
Mutagenesisi104S → A: 50% reduced protease activity. 1 Publication1
Mutagenesisi125S → A: Almost no protease activity. 1 Publication1
Mutagenesisi144S → A: No effect. 1 Publication1
Mutagenesisi160C → A or S: No protease activity. Cannot form complexes with HslU. 1 Publication1
Mutagenesisi173S → A: Almost no protease 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<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_00001481052 – 176ATP-dependent protease subunit HslVAdd BLAST175

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A7B8

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

More...PaxDbi		P0A7B8

PRoteomics IDEntifications database

More...PRIDEi		P0A7B8

2D gel databases

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

More...SWISS-2DPAGEi		P0A7B8

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By heat shock.UniRule annotation1 Publication

<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

A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.

UniRule annotation1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4261781, 287 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2104, HslUV protease complex

Database of interacting proteins

More...DIPi		DIP-35866N

Protein interaction database and analysis system

More...IntActi		P0A7B8, 33 interactors

STRING: functional protein association networks

More...STRINGi		511145.b3932

<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

1176
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		P0A7B8

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		P0A7B8

<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 information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase T1B family. HslV subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG5405, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_093872_1_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A7B8

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A7B8

Family and domain databases

Conserved Domains Database

More...CDDi		cd01913, protease_HslV, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.60.20.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00248, HslV, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR022281, ATP-dep_Prtase_HsIV_su
IPR029055, Ntn_hydrolases_N
IPR001353, Proteasome_sua/b
IPR023333, Proteasome_suB-type

The PANTHER Classification System

More...PANTHERi		PTHR32194, PTHR32194, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00227, Proteasome, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF039093, HslV, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56235, SSF56235, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR03692, ATP_dep_HslV, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51476, PROTEASOME_BETA_2, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7B8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTIVSVRRN GHVVIAGDGQ ATLGNTVMKG NVKKVRRLYN DKVIAGFAGG 
        60         70         80         90        100
TADAFTLFEL FERKLEMHQG HLVKAAVELA KDWRTDRMLR KLEALLAVAD 
       110        120        130        140        150
ETASLIITGN GDVVQPENDL IAIGSGGPYA QAAARALLEN TELSAREIAE 
       160        170 
KALDIAGDIC IYTNHFHTIE ELSYKA
Length:176
Mass (Da):19,093
Last modified:January 23, 2007 - v2
<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:i3B35E01F51486965
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
L19201 Genomic DNA Translation: AAB03064.1
U00096 Genomic DNA Translation: AAC76914.1
AP009048 Genomic DNA Translation: BAE77378.1
D89965 mRNA Translation: BAA14040.1 Sequence problems.
L14281 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...PIRi		JT0760

NCBI Reference Sequences

More...RefSeqi		NP_418367.1, NC_000913.3
WP_000208242.1, NZ_STEB01000017.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC76914; AAC76914; b3932
BAE77378; BAE77378; BAE77378

Database of genes from NCBI RefSeq genomes

More...GeneIDi		67417555
948429

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW3903
eco:b3932

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2773

<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
L19201 Genomic DNA Translation: AAB03064.1
U00096 Genomic DNA Translation: AAC76914.1
AP009048 Genomic DNA Translation: BAE77378.1
D89965 mRNA Translation: BAA14040.1 Sequence problems.
L14281 Genomic DNA No translation available.
PIRiJT0760
RefSeqiNP_418367.1, NC_000913.3
WP_000208242.1, NZ_STEB01000017.1

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
1E94X-ray2.80A/B/C/D2-176[»]
1G4AX-ray3.00A/B/C/D2-176[»]
1G4BX-ray7.00M/N/O/P2-176[»]
1HQYX-ray2.80A/B/C/D2-176[»]
1HT1X-ray2.80A/B/C/D/V/X/Y/Z2-176[»]
1HT2X-ray2.80A/B/C/D/I/J/K/L2-176[»]
1NEDX-ray3.80A/B/C2-176[»]
4G4EX-ray2.89A/B/C/D/E/F/G/H/I/J/K/L2-175[»]
5JI3X-ray3.00A/B/C/D1-176[»]
6PXIX-ray3.45A/B/C/D2-175[»]
SMRiP0A7B8
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261781, 287 interactors
ComplexPortaliCPX-2104, HslUV protease complex
DIPiDIP-35866N
IntActiP0A7B8, 33 interactors
STRINGi511145.b3932

Protein family/group databases

MEROPSiT01.006

2D gel databases

SWISS-2DPAGEiP0A7B8

Proteomic databases

jPOSTiP0A7B8
PaxDbiP0A7B8
PRIDEiP0A7B8

Genome annotation databases

EnsemblBacteriaiAAC76914; AAC76914; b3932
BAE77378; BAE77378; BAE77378
GeneIDi67417555
948429
KEGGiecj:JW3903
eco:b3932
PATRICifig|1411691.4.peg.2773

Organism-specific databases

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

More...EchoBASEi		EB1627

Phylogenomic databases

eggNOGiCOG5405, Bacteria
HOGENOMiCLU_093872_1_0_6
InParanoidiP0A7B8
PhylomeDBiP0A7B8

Enzyme and pathway databases

BioCyciEcoCyc:EG11676-MONOMER
BRENDAi3.4.25.2, 2026

Miscellaneous databases

EvolutionaryTraceiP0A7B8

Protein Ontology

More...PROi		PR:P0A7B8

Family and domain databases

CDDicd01913, protease_HslV, 1 hit
Gene3Di3.60.20.10, 1 hit
HAMAPiMF_00248, HslV, 1 hit
InterProiView protein in InterPro
IPR022281, ATP-dep_Prtase_HsIV_su
IPR029055, Ntn_hydrolases_N
IPR001353, Proteasome_sua/b
IPR023333, Proteasome_suB-type
PANTHERiPTHR32194, PTHR32194, 1 hit
PfamiView protein in Pfam
PF00227, Proteasome, 1 hit
PIRSFiPIRSF039093, HslV, 1 hit
SUPFAMiSSF56235, SSF56235, 1 hit
TIGRFAMsiTIGR03692, ATP_dep_HslV, 1 hit
PROSITEiView protein in PROSITE
PS51476, PROTEASOME_BETA_2, 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 nameiHSLV_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: P0A7B8
Secondary accession number(s): P31059, P97542, Q2M8M8
<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: June 7, 2005
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 141 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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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