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Entry version 94 (29 Sep 2021)
Sequence version 1 (01 Jun 2003)
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Protein

Collagenase ColT

Gene

colT

Organism
Clostridium tetani (strain Massachusetts / E88)
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

Clostridial collagenases are among the most efficient degraders of eukaryotic collagen known; saprophytes use collagen as a carbon source while pathogens additionally digest collagen to aid in host colonization. Has both tripeptidylcarboxypeptidase on Gly-X-Y and endopeptidase activities; the endopeptidase cuts within the triple helix region of collagen while tripeptidylcarboxypeptidase successively digests the exposed ends, thus clostridial collagenases can digest large sections of collagen (By similarity).

The activator domain (residues 57-330) and catalytic subdomain (340-611) open and close around substrate allowing digestion when the protein is closed (PubMed:23703618).

By similarity4 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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<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

Partially inhibited by 1-10-phenanthroline; inactivation is irreversible (PubMed:18937627, PubMed:23703618). Partially inhibited by EDTA; inactivation is reversible (PubMed:23703618). Inhibited by broad-spectrum zinc metalloprotease inhibitor batimastat (PubMed:28820255). N-aryl mercaptoacetamide-based inhibitors have been isolated that act on clostridial collagenases with submicromolar affinity while having negligibile activity on human collagenases (PubMed:28820255).3 Publications

<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

kcat is 7.24/sec, using a catalytic fragment (residues 53-727) on an artificial substrate.1 Publication
  1. KM=0.970 mM for furylacryloyl-Leu-Gly-Pro-Ala (FALGPA)1 Publication
  1. Vmax=5.53 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi440Calcium 1Combined sources1 Publication1
Metal bindingi465Zinc; catalytic; via tele nitrogenPROSITE-ProRule annotationCombined sources1 Publication1
<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 sitei466PROSITE-ProRule annotation1
Metal bindingi469Zinc; catalytic; via tele nitrogenPROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi473Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi477Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi479Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi499Zinc; catalyticCombined sources1 Publication1
Metal bindingi757Calcium 2By similarity1
Metal bindingi759Calcium 2By similarity1
Metal bindingi759Calcium 3By similarity1
Metal bindingi761Calcium 3By similarity1
Metal bindingi784Calcium 2By similarity1
Metal bindingi784Calcium 3By similarity1
Metal bindingi787Calcium 2By similarity1
Metal bindingi787Calcium 3By similarity1
Metal bindingi883Calcium 4By similarity1
Metal bindingi885Calcium 4By similarity1
Metal bindingi885Calcium 5By similarity1
Metal bindingi887Calcium 5By similarity1
Metal bindingi888Calcium 5By similarity1
Metal bindingi910Calcium 4By similarity1
Metal bindingi910Calcium 5By similarity1
Metal bindingi913Calcium 4By similarity1
Metal bindingi913Calcium 5By similarity1

<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, Metalloprotease, Protease
Biological processVirulence
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
CTET212717:G1G04-2798-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.3, 1526

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M09.005

<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:
Collagenase ColT1 Publication (EC:3.4.24.31 Publication)
Alternative name(s):
Microbial collagenase
<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:colT1 Publication
Ordered Locus Names:CTC_p33
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid pE88
<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>OrganismiClostridium tetani (strain Massachusetts / E88)
<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 identifieri212717 [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 lineageiBacteriaFirmicutesClostridiaEubacterialesClostridiaceaeClostridium
<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
  • UP000001412 <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: Plasmid pE88

<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

Secreted

<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

N-aryl mercaptoacetamide-based inhibitors with submicromolar affinity for clostridial collagenases but negligibile activity on human collagenases have been discovered that may lead to promising anti-infective drugs against Clostridia (PubMed:28820255).1 Publication

<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 – 28Sequence analysisAdd BLAST28
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000044354829 – 521 PublicationAdd BLAST24
<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_500430209353 – 991Collagenase ColTAdd BLAST939

Keywords - PTMi

Zymogen

<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

1991
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
Q899Y1

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>Regioni53 – 727S1 metalloprotease domain, degrades FALGPA (furylacryloyl-Leu-Gly-Pro-Ala)2 PublicationsAdd BLAST675
Regioni57 – 330Activator domain1 PublicationAdd BLAST274
Regioni340 – 611Catalytic subdomain1 PublicationAdd BLAST272
Regioni619 – 731Helper subdomain1 PublicationAdd BLAST113
Regioni755 – 870Collagen-binding domain 12 PublicationsAdd BLAST116
Regioni878 – 991Collagen-binding domain 22 PublicationsAdd BLAST114

<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 mature protein has 3 domains; a metalloprotease domain (S1, approximately residues 53 to 727) and 2 collagen-binding domains (CBD) (755-872) and (882-991) (PubMed:18937627). The metalloprotease S1 domain is composed of 3 subdomains which together resemble a saddle; an activator domain (residues 57-330), the catalytic peptidase subdomain (340-611) and a helper subdomain (619-731) (PubMed:23703618).1 Publication1 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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012279_0_0_9

Identification of Orthologs from Complete Genome Data

More...
OMAi
YEREGSY

Database of Orthologous Groups

More...
OrthoDBi
43759at2

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR041379, ColG_subdomain
IPR007280, Peptidase_C_arc/bac
IPR013661, Peptidase_M9_N_dom
IPR002169, Peptidase_M9A/M9B

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18496, ColG_sub, 1 hit
PF01752, Peptidase_M9, 1 hit
PF08453, Peptidase_M9_N, 1 hit
PF04151, PPC, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00931, MICOLLPTASE

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00142, ZINC_PROTEASE, 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.

<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 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.

Q899Y1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKKFIKMLC SIAIGCMIST SYSIKVSAFS NGNTKTNPNG EFKSLSLNST
60 70 80 90 100
NPYKTKYSFN DLNKLSNKEI LDLTSKIKWS DISDLFQYNK DSYTFYSNKE
110 120 130 140 150
RVQALIDGLY EKGCNYTSTD DKGIDTLVEI LRSGFYLGYY NDSLKYLNDK
160 170 180 190 200
SFKDKCIPAM IAIENNKNFK LGENGQDTVV HALGKLIGNT SCNDEVVNKT
210 220 230 240 250
IPILEQYYNE IDKYSKDRLK SNAVYNFMKE INYDISQYEY AHNIRDYKNT
260 270 280 290 300
PWSGKIDSFI DTISKFASIS NVTKDNGWII NNSIYYTAKL SKYHSNPSIP
310 320 330 340 350
HSVIDNCIEI FPDYSEQYFT AIEAIKEDFN SRDSKGNVID INKLIEEGKK
360 370 380 390 400
HYLPKTYTFD NGKIIIKAGD KVEESKIQKL YWASKEVKSQ FHRIIGNDKP
410 420 430 440 450
LEVGNADDIL TIVIYNNPEE YKLNKTLYGY SVDNGGIYIE GIGTFFTYER
460 470 480 490 500
TPQESIYSLE ELFRHEFTHY LQGRYLIPGL FNKGDFYKGN NGRITWFEEG
510 520 530 540 550
SAEFFAGSTR TSVLPRKSMV GGLSKNPKER FNADKLLHSK YSDGWDFYKY
560 570 580 590 600
GYAFSDYMYN NNKKLFSDLV STMKNNDVKG YEALIEESSK DSKINKDYEY
610 620 630 640 650
HMENLVNNYD NYTIPLVSDD YMKQYDNKSL HEIKSDIEKA MDVKNSQITK
660 670 680 690 700
ESSQYFDTYN LKATYTLSSN KGEISNWNYM NNKINEALNK LDNLSWGGYK
710 720 730 740 750
TVTAYFSNPR LNSNNEVVYD IVFHGLLSHN KNSNEKVEVK EEPEIKDKDS
760 770 780 790 800
FENVIYEKEN NDSFDKANKI HKNQIVMATL DTEDYRDTFY FDALTSGSID
810 820 830 840 850
ITIENIHGNS DAFNWLVYND EDLNNYIAYP TKKEDNKLMG SFKVHKPGRY
860 870 880 890 900
YILVYKTSLN KVNYKLNISD ATNMAPVIKK IHEKENNDSF ETANKITLDT
910 920 930 940 950
LVLGNLDYKD VSDIYSFDIE NTKDLNIKLT NLNNLGIAWN LYKESDLNNY
960 970 980 990
IAYGAKSDNA IVGKCNLSPG KYYLYVYKYS GDKGNYSVII N
Length:991
Mass (Da):114,376
Last modified:June 1, 2003 - 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:i9A5F57730134DED4
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
AF528097 Genomic DNA Translation: AAO37456.1

NCBI Reference Sequences

More...
RefSeqi
WP_011100838.1, NC_004565.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAO37456; AAO37456; CTC_p33

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ctc:CTC_p33

<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
AF528097 Genomic DNA Translation: AAO37456.1
RefSeqiWP_011100838.1, NC_004565.1

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
4AR8X-ray2.05A/B340-730[»]
4AR9X-ray1.69A/B340-730[»]
SMRiQ899Y1
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

MEROPSiM09.005

Genome annotation databases

EnsemblBacteriaiAAO37456; AAO37456; CTC_p33
KEGGictc:CTC_p33

Phylogenomic databases

HOGENOMiCLU_012279_0_0_9
OMAiYEREGSY
OrthoDBi43759at2

Enzyme and pathway databases

BioCyciCTET212717:G1G04-2798-MONOMER
BRENDAi3.4.24.3, 1526

Family and domain databases

InterProiView protein in InterPro
IPR041379, ColG_subdomain
IPR007280, Peptidase_C_arc/bac
IPR013661, Peptidase_M9_N_dom
IPR002169, Peptidase_M9A/M9B
PfamiView protein in Pfam
PF18496, ColG_sub, 1 hit
PF01752, Peptidase_M9, 1 hit
PF08453, Peptidase_M9_N, 1 hit
PF04151, PPC, 1 hit
PRINTSiPR00931, MICOLLPTASE
PROSITEiView protein in PROSITE
PS00142, ZINC_PROTEASE, 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 nameiCOLT_CLOTE
<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: Q899Y1
<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: March 28, 2018
Last sequence update: June 1, 2003
Last modified: September 29, 2021
This is version 94 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, Plasmid, 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
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