Skip Header

Contribute Send feedback
Read comments (?) or add your own

P42779 (BPRV_DICNO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Extracellular basic protease

EC=3.4.21.-
Gene names
Name:bprV
Synonyms:bpr
OrganismDichelobacter nodosus (Bacteroides nodosus)
Taxonomic identifier870 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCardiobacterialesCardiobacteriaceaeDichelobacter

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase S8 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 132111
PRO_0000026998
Chain133 – 476344Extracellular basic protease
PRO_0000026999
Propeptide477 – 603127
PRO_0000027000

Sites

Active site1731Charge relay system By similarity
Active site2371Charge relay system By similarity
Active site4091Charge relay system By similarity

Amino acid modifications

Disulfide bond221 ↔ 273 Ref.1
Disulfide bond315 ↔ 352 Ref.1

Sequences

Sequence LengthMass (Da)Tools
P42779 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F3919879E1142E2E

FASTA60363,869
        10         20         30         40         50         60 
MNLSNISAVK VLTLVVSAAI AGQVCAAESI VNYESANAIS KQPEGSVRFI VKYKDGTPSS 

        70         80         90        100        110        120 
QGLKTRSTTK VMASGMQVAG FEAQFVRTTG LGAGIFAVPE LKTTKEAHLV MDTIASNPDV 

       130        140        150        160        170        180 
EFVEVDRLAY PKAAPNDPSY RQQWHYFGNY GVKANKVWDR GFTGQGVVVS VVDTGILDHV 

       190        200        210        220        230        240 
DLNGNMLPGY DFISSAPNAR DGDQRDNNPA DEGDWFDNWD CGGYPDPRRE KKFSTWHGSH 

       250        260        270        280        290        300 
VAGTIAAVTN NGVGVAGVAY GAKVIPVRVL GKCGGYDSDI TDGMYWSAGG HIDGVPDNQN 

       310        320        330        340        350        360 
PAQVVNMSLG GGGGCSQNSQ RMIDKTTNLG ALIVIAAGNE NQDASRTWPS SCNNVLSVGA 

       370        380        390        400        410        420 
TTPKGKRAPF SNYGARVHLA APGTNILSTI DVGQAGPVRS SYGMKAGTSM AAPHVSGVAA 

       430        440        450        460        470        480 
LVISAANSIG KTLTPSELSD ILVRTTSRFN GRLDRGLGSG IVDANAAVNA VLGDQNRAQP 

       490        500        510        520        530        540 
RPPVNQPINS GNKVYRSDRR VAIRDLRSVT SGIRVNDQAR VGSANITLTL DIRYGDRSQL 

       550        560        570        580        590        600 
AVELIAPSGR VYPIYHDGKR QPNIVGPATF SVKNERLQGT WTLKVTDKAR GVTGSIDSWS 


LTF 

« Hide

References

[1]"Amino acid and DNA sequences of an extracellular basic protease of Dichelobacter nodosus show that it is a member of the subtilisin family of proteases."
Lilley G.G., Stewart D.J., Kortt A.A.
Eur. J. Biochem. 210:13-21(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: VCS 1001 / A198.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z16080 Genomic DNA. Translation: CAA78894.1.
PIRS27055.

3D structure databases

ProteinModelPortalP42779.
ModBaseSearch...

Protein family/group databases

MEROPSS08.022.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.200. 1 hit.
InterProIPR008979. Galactose-bd-like.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
[Graphical view]
PANTHERPTHR10795. PTHR10795. 1 hit.
PfamPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
SUPFAMSSF49785. Gal_bind_like. 1 hit.
SSF52743. Pept_S8_S53. 1 hit.
PROSITEPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBPRV_DICNO
AccessionPrimary (citable) accession number: P42779
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families