EzCatDB: T00257
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DB codeT00257
CATH domainDomain 13.40.50.10390 : Rossmann fold
Domain 23.40.50.1460 : Rossmann foldCatalytic domain
Domain 32.60.40.10 : Immunoglobulin-like
E.C.3.4.22.37
CSA1cvr

CATH domainRelated DB codes (homologues)
2.60.40.10 : Immunoglobulin-likeM00131,T00005,M00113,M00127,M00132,M00323,M00325,M00327,M00329,M00330,M00331,M00332,T00307,D00166,D00500,M00112,M00193,T00063,T00065,T00067,T00245
3.40.50.1460 : Rossmann foldD00522

Enzyme Name
UniProtKBKEGG

P95493
Protein nameGingipain R2gingipain R
Arg-gingipain
gingipain-1
argingipain
Arg-gingivain-55 proteinase
Arg-gingivain-70 proteinase
Arg-gingivain-75 proteinase
arginine-specific cysteine protease
arginine-specific gingipain
arginine-specific gingivain
RGP-1
RGP
SynonymsEC 3.4.22.37
Gingipain 2
Arg-gingipain
RGP-2
RefSeqNP_904801.1 (Protein)
NC_002950.2 (DNA/RNA sequence)
MEROPSC25.003 (Cysteine)
PfamPF01364 (Peptidase_C25)
PF03785 (Peptidase_C25_C)
PF08126 (Propeptide_C25)
[Graphical view]


UniProtKB:Accession NumberP95493
Entry nameCPG2_PORGI
ActivityHydrolysis of proteins and small molecule substrates, with a preference for Arg in P1.
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00017C00012C00001C00017C00012I00153I00154I00155
CompoundProteinPeptideH2OProteinPeptidePeptidyl-Cys-tetrahedral-intermediate (with previous peptide)Acyl-enzyme(Peptidyl-Cys-acyl group)Peptidyl-Cys-tetrahedral-intermediate
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein


ChEBI

15377





PubChem

962
22247451





                
1cvrA01UnboundUnbound UnboundUnboundUnboundUnboundUnbound
1cvrA02UnboundUnbound UnboundUnboundUnboundIntermediate-analogue:H37Unbound
1cvrA03UnboundUnbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P95493, literature [8]
pdbCatalytic residuesMain-chain involved in catalysis
          
1cvrA01 
 
1cvrA02GLU 152;HIS 211;CYS 244
GLY 212;CYS 244
1cvrA03 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[8]Fig.5, p.5457-5459

references
[1]
PubMed ID7864651
JournalArch Biochem Biophys
Year1995
Volume316
Pages917-25
AuthorsOkamoto K, Misumi Y, Kadowaki T, Yoneda M, Yamamoto K, Ikehara Y
TitleStructural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from Porphyromonas gingivalis.
[2]
PubMed ID7890369
JournalInfect Immun
Year1995
Volume63
Pages1176-82
AuthorsPotempa J, Pike R, Travis J
TitleThe multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain.
[3]
PubMed ID9467383
JournalOral Microbiol Immunol
Year1997
Volume12
Pages298-302
AuthorsAllaker RP, Aduse-Opoku J, Batten JE, Curtis MA
TitleNatural variation within the principal arginine-specific protease gene, prpR1, of Porphyromonas gingivalis.
[4]
PubMed ID9529086
JournalInfect Immun
Year1998
Volume66
Pages1594-600
AuthorsAduse-Opoku J, Rangarajan M, Young KA, Curtis MA
TitleMaturation of the arginine-specific proteases of Porphyromonas gingivalis W50 is dependent on a functional prR2 protease gene.
[5]
PubMed ID9605333
JournalProtein Sci
Year1998
Volume7
Pages1259-61
AuthorsBanbula A, Potempa J, Travis J, Bode W, Medrano FJ
TitleCrystallization and preliminary X-ray diffraction analysis of gingipain R2 from Porphyromonas gingivalis in complex with H-D-Phe-Phe-Arg-chloromethylketone.
[6]
PubMed ID9705298
JournalJ Biol Chem
Year1998
Volume273
Pages21648-57
AuthorsPotempa J, Mikolajczyk-Pawlinska J, Brassell D, Nelson D, Thogersen IB, Enghild JJ, Travis J
TitleComparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis.
[7]
PubMed ID10417143
JournalInfect Immun
Year1999
Volume67
Pages3816-23
AuthorsCurtis MA, Thickett A, Slaney JM, Rangarajan M, Aduse-Opoku J, Shepherd P, Paramonov N, Hounsell EF
TitleVariable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
PubMed ID10523290
JournalEMBO J
Year1999
Volume18
Pages5453-62
AuthorsEichinger A, Beisel HG, Jacob U, Huber R, Medrano FJ, Banbula A, Potempa J, Travis J, Bode W
TitleCrystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold.
Related PDB1cvr
Related UniProtKBP95493
[9]
PubMed ID10931897
JournalMicrobiology
Year2000
Volume146
Pages1933-40
AuthorsAduse-Opoku J, Davies NN, Gallagher A, Hashim A, Evans HE, Rangarajan M, Slaney JM, Curtis MA
TitleGeneration of lys-gingipain protease activity in Porphyromonas gingivalis W50 is independent of Arg-gingipain protease activities.
[10]
PubMed ID11278315
JournalJ Biol Chem
Year2001
Volume276
Pages18984-91
AuthorsImamura T, Banbula A, Pereira PJ, Travis J, Potempa J
TitleActivation of human prothrombin by arginine-specific cysteine proteinases (Gingipains R) from porphyromonas gingivalis.
[11]
PubMed ID11557483
JournalAntimicrob Agents Chemother
Year2001
Volume45
Pages2871-6
AuthorsImamura T, Matsushita K, Travis J, Potempa J
TitleInhibition of trypsin-like cysteine proteinases (gingipains) from Porphyromonas gingivalis by tetracycline and its analogues.
[12]
PubMed ID11139397
JournalBiochem J
Year2001
Volume353
Pages325-31
AuthorsImamura T, Tanase S, Hamamoto T, Potempa J, Travis J
TitleActivation of blood coagulation factor IX by gingipains R, arginine-specific cysteine proteinases from Porphyromonas gingivalis.
[13]
PubMed ID11160022
JournalInfect Immun
Year2001
Volume69
Pages1199-201
AuthorsRubinstein I, Potempa J, Travis J, Gao XP
TitleMechanisms mediating Porphyromonas gingivalis gingipain RgpA-induced oral mucosa inflammation in vivo.
[14]
PubMed ID14683426
JournalCurr Protein Pept Sci
Year2003
Volume4
Pages397-407
AuthorsPotempa J, Sroka A, Imamura T, Travis J
TitleGingipains, the major cysteine proteinases and virulence factors of Porphyromonas gingivalis: structure, function and assembly of multidomain protein complexes.
[15]
PubMed ID14529279
JournalBiochemistry
Year2003
Volume42
Pages11693-700
AuthorsAlly N, Whisstock JC, Sieprawska-Lupa M, Potempa J, Le Bonniec BF, Travis J, Pike RN
TitleCharacterization of the specificity of arginine-specific gingipains from Porphyromonas gingivalis reveals active site differences between different forms of the enzymes.

comments
This enzyme has got a catalytic domain, which is homologous to that of caspase-1 (D00522 in EzCatDB), with conserved catalytic residues.

createdupdated
2004-03-252012-10-23


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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