P95493 (CPG2_PORGI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Porphyromonas gingivalis (strain ATCC BAA-308 / W83) [Complete proteome] [HAMAP]

Taxonomic identifier

242619 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Bacteroidetes/Chlorobi group › Bacteroidetes › Bacteroidia › Bacteroidales › Porphyromonadaceae › Porphyromonas › Porphyromonas gingivalis

Protein attributes

Sequence length	736 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Virulence
Domain	Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Thiol protease
PTM	Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

By similarity

Propeptide

25 – 229

205

PRO_0000026535

Chain

230 – 736

507

Gingipain R2

PRO_0000026536

Sites

Active site

440

1

Proton donor

Active site

473

1

Nucleophile

Experimental info

Sequence conflict

58

1

G → D in AAB41892. Ref.1

Sequence conflict

246

1

P → A in AAB41892. Ref.1

Sequence conflict

251

1

E → G in AAB41892. Ref.1

Sequence conflict

254

1

E → K in AAB41892. Ref.1

Sequence conflict

398

1

I → V in AAB41892. Ref.1

Sequence conflict

435

1

A → V in AAB41892. Ref.1

Sequence conflict

480 – 482

3

YNV → FSM in AAB41892. Ref.1

Sequence conflict

510

1

N → D AA sequence Ref.1

Sequence conflict

512

1

S → Y AA sequence Ref.1

Sequence conflict

515

1

S → P AA sequence Ref.1

Sequence conflict

560

1

K → N in AAB41892. Ref.1

Sequence conflict

582

1

K → E in AAB41892. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

736

Helix Strand Turn

Details...

Beta strand

240 – 245

6

Helix

247 – 252

6

Helix

254 – 262

9

Beta strand

266 – 271

6

Helix

272 – 275

4

Helix

281 – 293

13

Beta strand

299 – 306

8

Turn

308 – 310

3

Beta strand

314 – 316

3

Beta strand

319 – 322

4

Helix

323 – 326

4

Beta strand

329 – 333

5

Beta strand

336 – 342

7

Helix

347 – 362

16

Turn

369 – 372

4

Beta strand

373 – 378

6

Helix

387 – 389

3

Helix

392 – 406

15

Beta strand

409 – 418

10

Helix

421 – 430

10

Beta strand

433 – 439

7

Beta strand

443 – 446

4

Turn

447 – 449

3

Turn

453 – 455

3

Helix

456 – 458

3

Beta strand

467 – 474

8

Beta strand

480 – 482

3

Helix

485 – 491

7

Beta strand

502 – 509

8

Helix

515 – 527

13

Helix

539 – 564

26

Beta strand

565 – 569

5

Beta strand

589 – 592

4

Beta strand

596 – 604

9

Beta strand

608 – 613

6

Beta strand

616 – 622

7

Beta strand

627 – 631

5

Beta strand

640 – 647

8

Beta strand

654 – 661

8

Sequences

	Sequence		Length	Mass (Da)
	P95493 [UniParc]. Last modified October 3, 2003. Version 2. Checksum: C848DD3FAB420833	FASTA	736	80,967
	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

References

	« Hide 'large scale' referencesShow '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. , 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).

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.

RefSeq

NP_904801.1. NC_002950.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CVR	X-ray	2.00	A	230-664	[»]

ProteinModelPortal

P95493.

SMR

P95493. Positions 230-661.

ModBase

Search...

Protein-protein interaction databases

STRING

242619.PG0506.

Protein family/group databases

MEROPS

C25.003.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAQ65700; AAQ65700; PG_0506.

GeneID

2552233.

KEGG

pgi:PG0506.

PATRIC

22978106. VBIPorGin134034_0464.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

NOG12793.

KO

K08589.

OMA

KENGRMI.

ProtClustDB

CLSK312019.

Enzyme and pathway databases

BioCyc

PGIN242619:GHX8-448-MONOMER.

BRENDA

3.4.22.37. 4997.

SABIO-RK

P95493.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.

InterPro

IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR001769. Peptidase_C25.
IPR005536. Peptidase_C25_Ig-like_domain.
IPR012600. Propeptide_C25.
IPR026444. Secre_tail.
[Graphical view]

Pfam

PF01364. Peptidase_C25. 1 hit.
PF03785. Peptidase_C25_C. 1 hit.
PF08126. Propeptide_C25. 1 hit.
[Graphical view]

SUPFAM

SSF81296. Ig_E-set. 1 hit.

TIGRFAMs

TIGR04183. Por_Secre_tail. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P95493.

Entry information

Entry name

CPG2_PORGI

Accession

Primary (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:	May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program