Reviewed, UniProtKB/Swiss-Prot P28784 (CPG1_PORGI)

Names and origin

Protein names

Recommended name:
    Gingipain R1
    EC=3.4.22.37
Alternative name(s):
    Gingipain 1
    Arg-gingipain
    RGP-1

Gene names

Name:	rgpA
Synonyms:	rgp1

Organism

Porphyromonas gingivalis (Bacteroides gingivalis)

Taxonomic identifier

837 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Porphyromonadaceae › Porphyromonas

Protein attributes

Sequence length	991 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.
Catalytic activity	Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1.
Enzyme regulation	Requires cysteine for activation and Ca2+ and/or Mg2+ for stabilization. It is stimulated by glycine-containing dipeptides. It is resistant to inhibition by proteinase inhibitors in human plasma.
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	Direct protein sequencing
Gene Ontology (GO)
Biological process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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
	Propeptide	25 – 227	203	Ref.1 Ref.2		PRO_0000026533
	Chain	228 – 991	764	Gingipain R1		PRO_0000026534
Sites
	Active site	438	1	Proton donor By similarity
	Active site	471	1	Nucleophile By similarity
Experimental info
	Sequence conflict	264 – 265	2	RT → TK AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P28784-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 03EE3F43CEBE2544	FASTA	991	108,782
	10 20 30 40 50 60 MKNLNKFVSI ALCSSLLGGM AFAQQTELGR NPNVRLLEST QQSVTKVQFR MDNLKFTEVQ 70 80 90 100 110 120 TPKGMAQVPT YTEGVNLSEK GMPTLPILSR SLAVSDTREM KVEVVSSKFI EKKNVLIAPS 130 140 150 160 170 180 KGMIMRNEDP KKIPYVYGKS YSQNKFFPGE IATLDDPFIL RDVRGQVVNF APLQYNPVTK 190 200 210 220 230 240 TLRIYTEITV AVSETSEQGK NILNKKGTFA GFEDTYKRMF MNYEPGRYTP VEEKQNGRMI 250 260 270 280 290 300 VIVAKKYEGD IKDFVDWKNQ RGLRTEVKVA EDIASPVTAN AIQQFVKQEY EKEGNDLTYV 310 320 330 340 350 360 LLVGDHKDIP AKITPGIKSD QVYGQIVGND HYNEVFIGRF SCESKEDLKT QIDRTIHYER 370 380 390 400 410 420 NITTEDKWLG QALCIASAEG GPSADNGESD IQHENVIANL LTQYGYTKII KCYDPGVTPK 430 440 450 460 470 480 NIIDAFNGGI SLVNYTGHGS ETAWGTSHFG TTHVKQLTNS NQLPFIFDVA CVNGDFLFSM 490 500 510 520 530 540 PCFAEALMRA QKDGKPTGTV AIIASTINQS WASPMRGQDE MNEILCEKHP NNIKRTFGGV 550 560 570 580 590 600 TMNGMFAMVE KYKKDGEKML DTWTVFGDPS LLVRTLVPTK MQVTAPAQIN LTDASVNVSC 610 620 630 640 650 660 DYNGAIATIS ANGKMFGSAV VENGTATINL TGLTNESTLT LTVVGYNKET VIKTINTNGE 670 680 690 700 710 720 PNPYQPVSNL TATTQGQKVT LKWDAPSTKT NATTNTARSV DGIRELVLLS VSDAPELLRS 730 740 750 760 770 780 GQAEIVLEAH DVWNDGSGYQ ILLDADHDQY GQVIPSDTHT LWPNCSVPAN LFAPFEYTVP 790 800 810 820 830 840 ENADPSCSPT NMIMDGTASV NIPAGTYDFA IAAPQANAKI WIAGQGPTKE DDYVFEAGKK 850 860 870 880 890 900 YHFLMKKMGS GDGTELTISE GGGSDYTYTV YRDGTKIKEG LTETTYRDAG MSAQSHEYCV 910 920 930 940 950 960 EVKYAAGVSP KVCVDYIPDG VADVTAQKPY TLTVVGKTIT VTCQGEAMIY DMNGRRLAAG 970 980 990 RNTVVYTAQG GYYAVMVVVD GKSYVEKLAV K

References

[1]

"Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from Porphyromonas gingivalis." Okamoto K., Misumi Y., Kadowaki T., Yoneda M., Yamamoto K., Ikehara Y. Arch. Biochem. Biophys. 316:917-925(1995) [PubMed: 7864651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 228-290 AND 517-541. Strain: 381.

[2]

"Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis." Chen Z., Potempa J., Polanowski A., Wikstrom M., Travis J. J. Biol. Chem. 267:18896-18901(1992) [PubMed: 1527017] [Abstract] Cited for: PROTEIN SEQUENCE OF 228-270. Strain: HG66.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D26470 Genomic DNA. Translation: BAA05484.1.
PIR	I40229.
3D structure databases
HSSP	HSSP built from PDB template 1CVR based on UniProtKB P95493.
SMR	P28784. Positions 228-655.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.4.22.37. 18777.
Family and domain databases
InterPro	IPR013783. Ig-like_fold. IPR018832. Pept_C25_gingipain_K. IPR001769. Peptidase_C25. IPR005536. Peptidase_C25_C. IPR012600. Propeptide_C25. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
Pfam	PF10365. DUF2436. 1 hit. PF01364. Peptidase_C25. 1 hit. PF03785. Peptidase_C25_C. 1 hit. PF08126. Propeptide_C25. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CPG1_PORGI

Accession

Primary (citable) accession number: P28784
Secondary accession number(s): Q45168

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	November 1, 1997
Last modified:	May 5, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)