Q51816 (Q51816_PORGN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Submitted name: Arg-gingipain-1 proteinase EMBL AAA69539.1
Organism	Porphyromonas gingivalis EMBL AAA69539.1
Taxonomic identifier	837 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Bacteroidetes/Chlorobi group › Bacteroidetes › Bacteroidia › Bacteroidales › Porphyromonadaceae › Porphyromonas

Protein attributes

Sequence length	1704 AA.
Sequence status	Complete.
Protein existence	Predicted

Ontologies

Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: InterPro
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
	Chain	228 – 719	492	mature 50-kDa cysteine proteinase gingipain EMBL AAA69539.1		PRO_5000144320

Sequences

	Sequence		Length	Mass (Da)
	Q51816 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 6A34B40131C2A676	FASTA	1,704	185,437
	10 20 30 40 50 60 MKNLNKFVSI ALCSSLLGGM AFAQQTELGR NPNVRLLEST QQSVTKVQFR MDNLKFTEVQ 70 80 90 100 110 120 TPKGIGQVPT 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 LTATTFEEDG VATGNHEYCV 910 920 930 940 950 960 EVKYTAGVSP KVCKDVTVEG SNEFAPVQNL TGSAVGQKVT LKWDAPNGTP NPNPNPNPNP 970 980 990 1000 1010 1020 GTTTLSESFE NGIPASWKTI DADGDGHGWK PGNAPGIAGY NSNGCVYSES FGLGGIGVLT 1030 1040 1050 1060 1070 1080 PDNYLITPAL DLPNGGKLTF WVCAQDANYA SEHYAVYASS TGNDASNFTN ALLEETITAK 1090 1100 1110 1120 1130 1140 GVRSPEAIRG RIQGTWRQKT VDLPAGTKYV AFRHFQSTDM FYIDLDEVEI KANGKRADFT 1150 1160 1170 1180 1190 1200 ETFESSTHGE APAEWTTIDA DGDGQGWLCL SSGQLDWLTA HGGTNVVASF SWNGMALNPD 1210 1220 1230 1240 1250 1260 NYLISKDVTG ATKVKYYYAV NDGFPGDHYA VMISKTGTNA GDFTVVFEET PNGINKGGAR 1270 1280 1290 1300 1310 1320 FGLSTEANGA KPQSVWIERT VDLPAGTKYV AFRHYNCSDL NYILLDDIQF TMGGSPTPTD 1330 1340 1350 1360 1370 1380 YTYTVYRDGT KIKEGLTETT FEEDGVATGN HEYCVEVKYT AGVSPKECVN VTINPTQFNP 1390 1400 1410 1420 1430 1440 VKNLKAQPDG GDVVLKWEAP SAKKTEGSRE VKRIGDGLFV TIEPANDVRA NEAKVVLAAD 1450 1460 1470 1480 1490 1500 NVWGDNTGYQ FLLDADHNTF GSVIPATGPL FTGTASSNLY SANFEYLIPA NADPVVTTQN 1510 1520 1530 1540 1550 1560 IIVTGQGEVV IPGGVYDYCI TNPEPASGKM WIAGDGGNQP ARYDDFTFEA GKKYTFTMRR 1570 1580 1590 1600 1610 1620 AGMGDGTDME VEDDSPASYT YTVYRDGTKI KEGLTETTYR DAGMSAQSHE YCVEVKYAAG 1630 1640 1650 1660 1670 1680 VSPKVCVDYI PDGVADVTAQ KPYTLTVVGK TITVTCQGEA MIYDMNGRRL AAGRNTVVYT 1690 1700 AQGGYYAVMV VVDGKSYVEK LAVK

References

[1]

"Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein." Pavloff N., Potempa J., Pike R.N., Prochazka V., Kiefer M.C., Travis J., Barr P.J. J. Biol. Chem. 270:1007-1010(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U15282 Genomic DNA. Translation: AAA69539.1.
PIR	A55426.
3D structure databases
HSSP	HSSP built from PDB template 1CVR based on UniProtKB P95493.
ProteinModelPortal	Q51816.
SMR	Q51816. Positions 228-655.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.60.40.10. 1 hit.
InterPro	IPR011628. Cleaved_adhesin. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. IPR018832. Pept_C25_gingipain_C. IPR001769. Peptidase_C25. IPR005536. Peptidase_C25_Ig-like_domain. IPR012600. Propeptide_C25. [Graphical view]
Pfam	PF07675. Cleaved_Adhesin. 2 hits. PF10365. DUF2436. 2 hits. 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.
ProtoNet	Search...

Entry information

Entry name

Q51816_PORGN

Accession

Primary (citable) accession number: Q51816

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)