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P95493 (CPG2_PORGI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gingipain R2

EC=3.4.22.37
Alternative name(s):
Arg-gingipain
Gingipain 2
RGP-2
Gene names
Name:rgpB
Synonyms:prtRII, rgp2
Ordered Locus Names:PG_0506
OrganismPorphyromonas gingivalis (strain ATCC BAA-308 / W83) [Complete proteome] [HAMAP]
Taxonomic identifier242619 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Protein attributes

Sequence length736 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Its proteolytic activity is a major factor in both periodontal tissue destruction and in bacterial host defense mechanisms. Activates complement C3 and C5 By similarity.

Catalytic activity

Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1.

Enzyme regulation

Inhibited by human histatin-3 1/24 (histatin-5). Ref.4

Sequence similarities

Belongs to the peptidase C25 family.

Ontologies

Keywords
   Biological processVirulence
   DomainSignal
   LigandCalcium
   Molecular functionHydrolase
Protease
Thiol protease
   PTMZymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HTN3P155167EBI-8505881,EBI-738783From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Propeptide25 – 229205
PRO_0000026535
Chain230 – 736507Gingipain R2
PRO_0000026536

Sites

Active site4401Proton donor
Active site4731Nucleophile

Experimental info

Sequence conflict581G → D in AAB41892. Ref.1
Sequence conflict2461P → A in AAB41892. Ref.1
Sequence conflict2511E → G in AAB41892. Ref.1
Sequence conflict2541E → K in AAB41892. Ref.1
Sequence conflict3981I → V in AAB41892. Ref.1
Sequence conflict4351A → V in AAB41892. Ref.1
Sequence conflict480 – 4823YNV → FSM in AAB41892. Ref.1
Sequence conflict5101N → D AA sequence Ref.1
Sequence conflict5121S → Y AA sequence Ref.1
Sequence conflict5151S → P AA sequence Ref.1
Sequence conflict5601K → N in AAB41892. Ref.1
Sequence conflict5821K → E in AAB41892. Ref.1

Secondary structure

........................................................................................................ 736
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P95493 [UniParc].

Last modified October 3, 2003. Version 2.
Checksum: C848DD3FAB420833

FASTA73680,967
        10         20         30         40         50         60 
MKKNFSRIVS IVAFSSLLGG MAFAQPAERG RNPQVRLLSA EQSMSKVQFR MDNLQFTGVQ 

        70         80         90        100        110        120 
TSKGVAQVPT FTEGVNISEK GTPILPILSR SLAVSETRAM KVEVVSSKFI EKKDVLIAPS 

       130        140        150        160        170        180 
KGVISRAENP DQIPYVYGQS YNEDKFFPGE IATLSDPFIL RDVRGQVVNF APLQYNPVTK 

       190        200        210        220        230        240 
TLRIYTEIVV AVSETAEAGQ NTISLVKNST FTGFEDIYKS VFMNYEATRY TPVEEKENGR 

       250        260        270        280        290        300 
MIVIVPKKYE EDIEDFVDWK NQRGLRTEVK VAEDIASPVT ANAIQQFVKQ EYEKEGNDLT 

       310        320        330        340        350        360 
YVLLVGDHKD IPAKITPGIK SDQVYGQIVG NDHYNEVFIG RFSCESKEDL KTQIDRTIHY 

       370        380        390        400        410        420 
ERNITTEDKW LGQALCIASA EGGPSADNGE SDIQHENIIA NLLTQYGYTK IIKCYDPGVT 

       430        440        450        460        470        480 
PKNIIDAFNG GISLANYTGH GSETAWGTSH FGTTHVKQLT NSNQLPFIFD VACVNGDFLY 

       490        500        510        520        530        540 
NVPCFAEALM RAQKDGKPTG TVAIIASTIN QSWASPMRGQ DEMNEILCEK HPNNIKRTFG 

       550        560        570        580        590        600 
GVTMNGMFAM VEKYKKDGEK MLDTWTVFGD PSLLVRTLVP TKMQVTAPAN ISASAQTFEV 

       610        620        630        640        650        660 
ACDYNGAIAT LSDDGDMVGT AIVKDGKAII KLNESIADET NLTLTVVGYN KVTVIKDVKV 

       670        680        690        700        710        720 
EGTSIADVAN DKPYTVAVSG KTITVESPAA GLTIFDMNGR RVATAKNRMV FEAQNGVYAV 

       730 
RIATEGKTYT EKVIVK 

« Hide

References

« Hide 'large scale' references
[1]"Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis."
Potempa J., Mikolajczyk-Pawlinska J., Brassell D., Nelson D., Thoegersen I.B., Enghild J.J., Travis J.
J. Biol. Chem. 273:21648-21657(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 230-651.
Strain: HG66.
[2]"Characterization of a second cell-associated Arg-specific cysteine proteinase of Porphyromonas gingivalis and identification of an adhesin-binding motif involved in association of the prtR and prtK proteinases and adhesins into large complexes."
Slakeski N., Bhogal P.S., O'Brien-Simpson N.M., Reynolds E.C.
Microbiology 144:1583-1592(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 53978 / W50.
[3]"Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83."
Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J., Granger D., Tettelin H. expand/collapse author list , Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E., Fraser C.M.
J. Bacteriol. 185:5591-5601(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-308 / W83.
[4]"Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease."
Gusman H., Travis J., Helmerhorst E.J., Potempa J., Troxler R.F., Oppenheim F.G.
Infect. Immun. 69:1402-1408(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[5]"Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold."
Eichinger A., Beisel H.-G., Jacob U., Huber R., Medrano F.-J., Banbula A., Potempa J., Travis J., Bode W.
EMBO J. 18:5453-5462(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85038 Genomic DNA. Translation: AAB41892.1.
AF007124 Genomic DNA. Translation: AAC26371.1.
AE015924 Genomic DNA. Translation: AAQ65700.1.
RefSeqNP_904801.1. NC_002950.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CVRX-ray2.00A230-664[»]
4IEFX-ray2.30A/C/E/G25-229[»]
B/D/F/H230-662[»]
ProteinModelPortalP95493.
SMRP95493. Positions 230-661.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP95493. 1 interaction.
MINTMINT-8415911.
STRING242619.PG0506.

Protein family/group databases

MEROPSC25.003.

Proteomic databases

PRIDEP95493.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ65700; AAQ65700; PG_0506.
GeneID2552233.
KEGGpgi:PG0506.
PATRIC22978106. VBIPorGin134034_0464.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG12793.
KOK08589.
OMAKENGRMI.
OrthoDBEOG6BGNW2.
ProtClustDBCLSK312019.

Enzyme and pathway databases

BioCycPGIN242619:GHX8-458-MONOMER.
BRENDA3.4.22.37. 4997.
SABIO-RKP95493.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR001769. Gingipain.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR005536. Peptidase_C25_Ig-like_domain.
IPR012600. Propeptide_C25.
IPR026444. Secre_tail.
[Graphical view]
PfamPF01364. Peptidase_C25. 1 hit.
PF03785. Peptidase_C25_C. 1 hit.
PF08126. Propeptide_C25. 1 hit.
[Graphical view]
SUPFAMSSF81296. SSF81296. 1 hit.
TIGRFAMsTIGR04183. Por_Secre_tail. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP95493.

Entry information

Entry nameCPG2_PORGI
AccessionPrimary (citable) accession number: P95493
Secondary accession number(s): O33441
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 3, 2003
Last modified: April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references