NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 228-290 AND 517-541.
STRAIN=381;
DOI=10.1006/abbi.1995.1123; PubMed=7864651 [NCBI, ExPASy, EBI, Israel, Japan]
Okamoto K., Misumi Y., Kadowaki T., Yoneda M., Yamamoto K., Ikehara Y.;
"Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogenic factor from Porphyromonas gingivalis.";
Arch. Biochem. Biophys. 316:917-925(1995).

[2]

PROTEIN SEQUENCE OF 228-270.
STRAIN=HG66;
PubMed=1527017 [NCBI, ExPASy, EBI, Israel, Japan]
Chen Z., Potempa J., Polanowski A., Wikstrom M., Travis J.;
"Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis.";
J. Biol. Chem. 267:18896-18901(1992).

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 Ca(2+) and/or Mg(2+) for stabilization. It is stimulated by glycine-containing dipeptides. It is resistant to inhibition by proteinase inhibitors in human plasma.
SIMILARITY: Belongs to the peptidase C25 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D26470; BAA05484.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I40229; I40229.

3D structure databases

HSSP

P95493; 1CVR. [HSSP ENTRY / PDB]

SMR

P28784; 228-655.

ModBase

P28784.

Ontologies

GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004197;	Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR013783; Ig-like_fold.
IPR001769; Peptidase_C25.
IPR005536; Peptidase_C25_C.
IPR012600; Propeptide_C25.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.10; Ig-like_fold; 1.

Pfam

PF01364; Peptidase_C25; 1.
PF03785; Peptidase_C25_C; 1.
PF08126; Propeptide_C25; 1.
Pfam graphical view of domain structure.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Direct protein sequencing; Hydrolase; Protease; Signal; Thiol protease; Virulence; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`
`PROPEP`	`25 227`	`203`		`PRO_0000026533`
`CHAIN`	`228 991`	`764`	`Gingipain R1.`	`PRO_0000026534`
`ACT_SITE`	`438 438`		`Proton donor (By similarity).`
`ACT_SITE`	`471 471`		`Nucleophile (By similarity).`
`CONFLICT`	`264 265`		`RT -> TK (in Ref. 2; AA sequence).`

Sequence information

Length: 991 AA [This is the length of the unprocessed precursor]

Molecular weight: 108782 Da [This is the MW of the unprocessed precursor]

CRC64: 03EE3F43CEBE2544 [This is a checksum on the sequence]

        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

P28784 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools