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 147 (11 Dec 2019)
Sequence version 3 (15 Jul 1998)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

ATP-dependent Clp protease proteolytic subunit

Gene

clpP

Organism
Bacillus subtilis (strain 168)
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

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX (PubMed:20305655). Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor (PubMed:16899079). Probably the major protease that degrades proteins tagged by trans-translation (PubMed:11395451, PubMed:31155236).UniRule annotation4 Publications

<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

  • Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).UniRule annotation1 Publication EC:3.4.21.92

<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

Low intrinsic peptidase activity is stimulated by ATP-binding subunits ClpC, ClpE and ClpX. Activity is disregulated by acyldepsipeptides (ADEP) antibiotics, which negate the need for ATP-binding subunits for activation and which makes it into an unregulated protease. Each ClpP subunit binds 1 ADEP molecule, which prevents binding of ClpX. ADEP binding causes conformational shifts that open the gated pore of the ring (PubMed:20305655). Protease activity is inhibited by diisopropylfluoro-phosphate (PubMed:22080375). Protease activity is inhibited by bortezomib, an oncology drug originally designed to work on the human proteasome (PubMed:31155236).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei98NucleophileUniRule annotation1 Publication1
Active sitei123UniRule annotation1 Publication1

<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

<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, Serine protease
Biological processStress response

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU34540-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.21.92 658

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S14.001

<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_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:
ATP-dependent Clp protease proteolytic subunitUniRule annotation (EC:3.4.21.92UniRule annotation1 Publication)
Alternative name(s):
Caseinolytic protease
Endopeptidase ClpUniRule annotation
Stress protein G7
<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:clpPUniRule annotation
Synonyms:yvdN
Ordered Locus Names:BSU34540
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<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
  • UP000001570 <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

<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

No degradation of trans-translationally tagged-peptides (PubMed:11395451, PubMed:31155236). Triple rqcH clpP ssrA mutants cannot be generated (ssrA, or tmRNA, encodes the SsrA tag added to nascent proteins in stalled ribosomes by trans-translation, targeting the nascent protein for degradation) (PubMed:31155236).2 Publications

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>Mutagenesisi20I → C or S: Protein no longer oligomerizes, loss of protease activity. 1 Publication1
Mutagenesisi25L → S: Protein no longer oligomerizes, loss of protease activity. 1 Publication1
Mutagenesisi46S → C: Has peptidase but not protease activity, activated by ADEP antibiotics. 1 Publication1
Mutagenesisi50F → S: Protein no longer oligomerizes, loss of protease activity, activated by ADEP antibiotics. 1 Publication1
Mutagenesisi54E → R: Has peptidase but not protease activity, activated by ADEP antibiotics. 1 Publication1
Mutagenesisi63Y → A: Has peptidase but not protease activity, partially activated by ADEP antibiotics. 1 Publication1
Mutagenesisi63Y → W: Has peptidase but not protease activity. 1 Publication1
Mutagenesisi83F → A: Has peptidase but not protease activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2146309

<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_00001795011 – 197ATP-dependent Clp protease proteolytic subunitAdd BLAST197

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P80244

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

More...
PaxDbi
P80244

PRoteomics IDEntifications database

More...
PRIDEi
P80244

<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, salt stress, ethanol stress, oxidative stress, glucose limitation and oxygen limitation.3 Publications

<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

Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes (PubMed:20305655, PubMed:22080375). Forms large heterooligomeric complexes consisting of an ATPase component (ClpX, ClpC or ClpE) and a proteolytic component (ClpP)(PubMed:20305655).

UniRule annotation2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-8165631,EBI-8165631

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-43711N

Protein interaction database and analysis system

More...
IntActi
P80244, 1 interactor

Molecular INTeraction database

More...
MINTi
P80244

STRING: functional protein association networks

More...
STRINGi
224308.BSU34540

<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

1197
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
P80244

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
P80244

<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

Peptide exit pores open in the compressed state; in this conformation the active site residues move apart and the protease cannot be active.1 Publication

<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 S14 family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CCQ Bacteria
COG0740 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000285833

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P80244

KEGG Orthology (KO)

More...
KOi
K01358

Identification of Orthologs from Complete Genome Data

More...
OMAi
GIFDTMQ

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P80244

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07017 S14_ClpP_2, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00444 ClpP, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001907 ClpP
IPR029045 ClpP/crotonase-like_dom_sf
IPR023562 ClpP/TepA
IPR033135 ClpP_His_AS
IPR018215 ClpP_Ser_AS

The PANTHER Classification System

More...
PANTHERi
PTHR10381 PTHR10381, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00574 CLP_protease, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00127 CLPPROTEASEP

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52096 SSF52096, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00493 clpP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00382 CLP_PROTEASE_HIS, 1 hit
PS00381 CLP_PROTEASE_SER, 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.

P80244-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNLIPTVIEQ TNRGERAYDI YSRLLKDRII MLGSAIDDNV ANSIVSQLLF
60 70 80 90 100
LAAEDPEKEI SLYINSPGGS ITAGMAIYDT MQFIKPKVST ICIGMAASMG
110 120 130 140 150
AFLLAAGEKG KRYALPNSEV MIHQPLGGAQ GQATEIEIAA KRILLLRDKL
160 170 180 190
NKVLAERTGQ PLEVIERDTD RDNFKSAEEA LEYGLIDKIL THTEDKK
Length:197
Mass (Da):21,682
Last modified:July 15, 1998 - v3
<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:i5D4D4BD548DC45A0
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
U59754 Genomic DNA Translation: AAC46381.1
Z94043 Genomic DNA Translation: CAB08043.1
AL009126 Genomic DNA Translation: CAB15459.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B69601

NCBI Reference Sequences

More...
RefSeqi
NP_391334.1, NC_000964.3
WP_003228214.1, NZ_JNCM01000033.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB15459; CAB15459; BSU34540

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
938625

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU34540

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.3741

<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
U59754 Genomic DNA Translation: AAC46381.1
Z94043 Genomic DNA Translation: CAB08043.1
AL009126 Genomic DNA Translation: CAB15459.1
PIRiB69601
RefSeqiNP_391334.1, NC_000964.3
WP_003228214.1, NZ_JNCM01000033.1

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
3KTGX-ray2.40A/B/C/D/E/F/G2-197[»]
3KTHX-ray3.00A/B/C/D/E/F/G2-197[»]
3KTIX-ray2.00A/B/C/D/E/F/G2-197[»]
3KTJX-ray2.60A/B/C/D/E/F/G2-197[»]
3KTKX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N2-197[»]
3TT6X-ray2.59A/B/C/D/E/F/G2-197[»]
3TT7X-ray2.56A/B/C/D/E/F/G1-197[»]
SMRiP80244
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-43711N
IntActiP80244, 1 interactor
MINTiP80244
STRINGi224308.BSU34540

Chemistry databases

ChEMBLiCHEMBL2146309

Protein family/group databases

MEROPSiS14.001

Proteomic databases

jPOSTiP80244
PaxDbiP80244
PRIDEiP80244

Genome annotation databases

EnsemblBacteriaiCAB15459; CAB15459; BSU34540
GeneIDi938625
KEGGibsu:BSU34540
PATRICifig|224308.179.peg.3741

Phylogenomic databases

eggNOGiENOG4105CCQ Bacteria
COG0740 LUCA
HOGENOMiHOG000285833
InParanoidiP80244
KOiK01358
OMAiGIFDTMQ
PhylomeDBiP80244

Enzyme and pathway databases

BioCyciBSUB:BSU34540-MONOMER
BRENDAi3.4.21.92 658

Miscellaneous databases

EvolutionaryTraceiP80244

Family and domain databases

CDDicd07017 S14_ClpP_2, 1 hit
HAMAPiMF_00444 ClpP, 1 hit
InterProiView protein in InterPro
IPR001907 ClpP
IPR029045 ClpP/crotonase-like_dom_sf
IPR023562 ClpP/TepA
IPR033135 ClpP_His_AS
IPR018215 ClpP_Ser_AS
PANTHERiPTHR10381 PTHR10381, 1 hit
PfamiView protein in Pfam
PF00574 CLP_protease, 1 hit
PRINTSiPR00127 CLPPROTEASEP
SUPFAMiSSF52096 SSF52096, 1 hit
TIGRFAMsiTIGR00493 clpP, 1 hit
PROSITEiView protein in PROSITE
PS00382 CLP_PROTEASE_HIS, 1 hit
PS00381 CLP_PROTEASE_SER, 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 nameiCLPP_BACSU
<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: P80244
Secondary accession number(s): O08433
<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: February 1, 1995
Last sequence update: July 15, 1998
Last modified: December 11, 2019
This is version 147 of the entry and version 3 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Peptidase families
    Classification of peptidase families and list of entries
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