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 138 (02 Jun 2021)
Sequence version 1 (01 Jan 1998)
Previous versions | rss
Add a publicationFeedback
Protein

Carboxy-terminal processing protease CtpB

Gene

ctpB

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

Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the pre-processed regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation.

4 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

  • The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.1 Publication EC:3.4.21.102

<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

Activated by peptide binding to the PDZ domain.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei168Crucial for substrate binding and protease activation1 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 sitei309Nucleophile1 Publication1
Active sitei334Charge relay system1 Publication1
Active sitei338Charge relay system1 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

  • endopeptidase activity Source: GO_Central
  • identical protein binding Source: IntAct
  • peptidase activity Source: UniProtKB
  • peptide binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • serine-type endopeptidase activity Source: UniProtKB-EC

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 processSporulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU35240-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.21.102, 658

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S41.007

Transport Classification Database

More...
TCDBi
9.B.174.1.1, the two tunnel gated c-terminal processing protease (ctp) family

<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:
Carboxy-terminal processing protease CtpB (EC:3.4.21.1021 Publication)
Short name:
C-terminal processing protease
<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:ctpB
Synonyms:yvjB
Ordered Locus Names:BSU35240
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<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
  • UP000001570 <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

<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

Pro-sigma-K processing is delayed by approximately 30 minutes, and sporulation efficiency is reduced approximately two-fold.3 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>Mutagenesisi36 – 40AAVPA → RAVPR: No cleavage by SpoIVB. No effect on pro-sigma-K processing. 1 Publication5
Mutagenesisi92 – 182Missing : Constitutively active protease with higher activity than wild-type protease and total loss of substrate specificity. 1 PublicationAdd BLAST91
Mutagenesisi118V → Y: Loss of peptide binding to the PDZ domain, but still has residual protease activity. Less than residual protease activity; when associated with A/F-168. 1 Publication1
Mutagenesisi168R → A or F: 3- to 5-fold weaker affinity for PDZ ligands and reduced proteolytic activity against pre-processed SpoIVFA substrate. Less than residual protease activity; when associated with Y-118. 1 Publication1
Mutagenesisi309S → A: Loss of activity. 1 Publication1
Mutagenesisi338Q → E: Loss of 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23Sequence analysisAdd BLAST23
<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_000039077724 – 480Carboxy-terminal processing protease CtpBAdd BLAST457

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Is cleaved by SpoIVB in vitro and in vivo but this cleavage does not appear to be necessary for CtpB activation. CtpB can also cleave itself in vivo.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei36 – 37Cleavage; by SpoIVB, and cleavage; by autolysis1 Publication2
Sitei40 – 41Cleavage; by SpoIVB2
Sitei42 – 43Cleavage; by autolysis1 Publication2

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

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

More...
PaxDbi
O35002

PRoteomics IDEntifications database

More...
PRIDEi
O35002

<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 provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Is expressed in the forespore under the control of sigma-G, and in the mother cell under the control of sigma-E.2 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%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

Homodimer.

1 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

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
O35002, 3 interactors

STRING: functional protein association networks

More...
STRINGi
224308.BSU35240

<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

1480
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
O35002

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini92 – 182PDZPROSITE-ProRule annotationAdd BLAST91

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>Regioni113 – 116Peptide binding1 Publication4

<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

The PDZ domain functions as a gatekeeper to the protease tunnel and defines resting and active conformations of the protease.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 S41A family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0793, Bacteria
COG3409, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O35002

Identification of Orthologs from Complete Genome Data

More...
OMAi
DPHSSYY

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O35002

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07560, Peptidase_S41_CPP, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.101.10, 1 hit
2.30.42.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029045, ClpP/crotonase-like_dom_sf
IPR001478, PDZ
IPR041489, PDZ_6
IPR036034, PDZ_sf
IPR004447, Peptidase_S41A
IPR002477, Peptidoglycan-bd-like
IPR036365, PGBD-like_sf
IPR036366, PGBDSf
IPR005151, Tail-specific_protease

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17820, PDZ_6, 1 hit
PF03572, Peptidase_S41, 1 hit
PF01471, PG_binding_1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00228, PDZ, 1 hit
SM00245, TSPc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47090, SSF47090, 1 hit
SSF50156, SSF50156, 1 hit
SSF52096, SSF52096, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00225, prc, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50106, PDZ, 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.

O35002-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNQKIMAVIA AGSMLFGGAG VYAGINLLEM DKPQTAAVPA TAQADSERDK
60 70 80 90 100
AMDKIEKAYE LISNEYVEKV DREKLLEGAI QGMLSTLNDP YSVYMDKQTA
110 120 130 140 150
KQFSDSLDSS FEGIGAEVGM EDGKIIIVSP FKKSPAEKAG LKPNDEIISI
160 170 180 190 200
NGESMAGKDL NHAVLKIRGK KGSSVSMKIQ RPGTKKQLSF RIKRAEIPLE
210 220 230 240 250
TVFASEKKVQ GHSVGYIAIS TFSEHTAEDF AKALRELEKK EIEGLVIDVR
260 270 280 290 300
GNPGGYLQSV EEILKHFVTK DQPYIQIAER NGDKKRYFST LTHKKAYPVN
310 320 330 340 350
VITDKGSASA SEILAGALKE AGHYDVVGDT SFGKGTVQQA VPMGDGSNIK
360 370 380 390 400
LTLYKWLTPN GNWIHKKGIE PTIAIKQPDY FSAGPLQLKE PLKVDMNNED
410 420 430 440 450
VKHAQVLLKG LSFDPGREDG YFSKDMKKAV MAFQDQNKLN KTGVIDTRTA
460 470 480
ETLNQQIEKK KSDEKNDLQL QTALKSLFVN
Length:480
Mass (Da):52,798
Last modified:January 1, 1998 - 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:i902B082C85B5CEC4
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
AF017113 Genomic DNA Translation: AAC67263.1
AL009126 Genomic DNA Translation: CAB15541.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E70042

NCBI Reference Sequences

More...
RefSeqi
NP_391404.1, NC_000964.3
WP_003228041.1, NZ_JNCM01000033.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB15541; CAB15541; BSU_35240

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
936678

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU35240

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.3814

<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
AF017113 Genomic DNA Translation: AAC67263.1
AL009126 Genomic DNA Translation: CAB15541.1
PIRiE70042
RefSeqiNP_391404.1, NC_000964.3
WP_003228041.1, 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
4C2CX-ray1.90A44-480[»]
4C2DX-ray2.70A/B/C/D44-480[»]
4C2EX-ray1.80A/B44-480[»]
4C2FX-ray2.40A44-480[»]
4C2GX-ray1.90A44-480[»]
C29-40[»]
4C2HX-ray1.95A/B44-480[»]
SMRiO35002
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiO35002, 3 interactors
STRINGi224308.BSU35240

Protein family/group databases

MEROPSiS41.007
TCDBi9.B.174.1.1, the two tunnel gated c-terminal processing protease (ctp) family

Proteomic databases

PaxDbiO35002
PRIDEiO35002

Genome annotation databases

EnsemblBacteriaiCAB15541; CAB15541; BSU_35240
GeneIDi936678
KEGGibsu:BSU35240
PATRICifig|224308.179.peg.3814

Phylogenomic databases

eggNOGiCOG0793, Bacteria
COG3409, Bacteria
InParanoidiO35002
OMAiDPHSSYY
PhylomeDBiO35002

Enzyme and pathway databases

BioCyciBSUB:BSU35240-MONOMER
BRENDAi3.4.21.102, 658

Family and domain databases

CDDicd07560, Peptidase_S41_CPP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.30.42.10, 1 hit
InterProiView protein in InterPro
IPR029045, ClpP/crotonase-like_dom_sf
IPR001478, PDZ
IPR041489, PDZ_6
IPR036034, PDZ_sf
IPR004447, Peptidase_S41A
IPR002477, Peptidoglycan-bd-like
IPR036365, PGBD-like_sf
IPR036366, PGBDSf
IPR005151, Tail-specific_protease
PfamiView protein in Pfam
PF17820, PDZ_6, 1 hit
PF03572, Peptidase_S41, 1 hit
PF01471, PG_binding_1, 1 hit
SMARTiView protein in SMART
SM00228, PDZ, 1 hit
SM00245, TSPc, 1 hit
SUPFAMiSSF47090, SSF47090, 1 hit
SSF50156, SSF50156, 1 hit
SSF52096, SSF52096, 1 hit
TIGRFAMsiTIGR00225, prc, 1 hit
PROSITEiView protein in PROSITE
PS50106, PDZ, 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 nameiCTPB_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: O35002
Secondary accession number(s): Q795D7
<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: January 19, 2010
Last sequence update: January 1, 1998
Last modified: June 2, 2021
This is version 138 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. 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

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