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Protein

Lys-gingipain W83

Gene

kgp

Organism
Porphyromonas gingivalis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria (By similarity).By similarity

Catalytic activityi

Endopeptidase with strict specificity for lysyl bonds.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei444 – 4441Proton donorBy similarity
Active sitei477 – 4771NucleophileBy similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Virulence

Protein family/group databases

MEROPSiC25.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Lys-gingipain W831 PublicationBy similarity (EC:3.4.22.47)
Alternative name(s):
Lysine specific cysteine protease1 PublicationImported
Lysine-specific cysteine proteinase1 PublicationImported
Porphypain1 PublicationImported
PrtK481 Publication
Cleaved into the following 4 chains:
Lys-gingipain catalytic subunit1 PublicationBy similarity
39 kDa adhesin1 Publication
Alternative name(s):
PrtK391 Publication
15 kDa adhesin1 Publication
Alternative name(s):
PrtK151 Publication
44 kDa adhesin1 Publication
Alternative name(s):
PrtK441 Publication
Gene namesi
Name:kgpBy similarity
Synonyms:prtKImported, prtP1 PublicationImported
OrganismiPorphyromonas gingivalis
Taxonomic identifieri837 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Subcellular locationi

Chain Lys-gingipain catalytic subunit : Secretedextracellular space By similarity

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Propeptidei25 – 228204Sequence Analysis1 PublicationPRO_0000395381Add
BLAST
Chaini229 – 17321504Lys-gingipain W831 PublicationPRO_0000395382Add
BLAST
Chaini229 – ?Lys-gingipain catalytic subunit1 PublicationPRO_0000395383
Chaini738 – ?39 kDa adhesin1 PublicationPRO_0000395384
Chaini1157 – ?15 kDa adhesin1 PublicationPRO_0000395385
Chaini1292 – ?44 kDa adhesin1 PublicationPRO_0000395386

Post-translational modificationi

Proteolytically cleaved into a catalytic subunit and three adhesins. Arg-gingipain is involved in this post-translational processing.By similarity1 Publication

Keywords - PTMi

Zymogen

Structurei

Secondary structure

1
1732
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi230 – 2334Combined sources
Beta strandi240 – 2489Combined sources
Helixi250 – 2523Combined sources
Helixi253 – 26513Combined sources
Beta strandi268 – 2747Combined sources
Turni278 – 2803Combined sources
Helixi284 – 30017Combined sources
Beta strandi306 – 3127Combined sources
Turni314 – 3163Combined sources
Turni323 – 3253Combined sources
Beta strandi327 – 3304Combined sources
Helixi331 – 3344Combined sources
Beta strandi337 – 3415Combined sources
Beta strandi343 – 3497Combined sources
Helixi354 – 36916Combined sources
Helixi375 – 3795Combined sources
Beta strandi380 – 3856Combined sources
Helixi391 – 3944Combined sources
Helixi396 – 40611Combined sources
Helixi410 – 4123Combined sources
Beta strandi415 – 4206Combined sources
Turni426 – 4294Combined sources
Helixi430 – 4345Combined sources
Beta strandi437 – 4437Combined sources
Turni451 – 4544Combined sources
Helixi457 – 4615Combined sources
Beta strandi470 – 4789Combined sources
Beta strandi484 – 4863Combined sources
Helixi489 – 4957Combined sources
Beta strandi499 – 50911Combined sources
Helixi513 – 5219Combined sources
Turni533 – 5353Combined sources
Helixi540 – 5456Combined sources
Beta strandi547 – 5493Combined sources
Helixi553 – 56917Combined sources
Helixi578 – 5847Combined sources
Beta strandi585 – 5895Combined sources
Beta strandi616 – 6227Combined sources
Beta strandi627 – 6326Combined sources
Beta strandi635 – 6428Combined sources
Beta strandi646 – 6549Combined sources
Beta strandi660 – 6678Combined sources
Beta strandi674 – 6807Combined sources
Beta strandi984 – 9874Combined sources
Beta strandi997 – 10015Combined sources
Beta strandi1010 – 10134Combined sources
Turni1014 – 10163Combined sources
Beta strandi1022 – 103211Combined sources
Turni1033 – 10364Combined sources
Beta strandi1043 – 10464Combined sources
Beta strandi1056 – 106611Combined sources
Beta strandi1073 – 10819Combined sources
Helixi1085 – 10873Combined sources
Beta strandi1090 – 10967Combined sources
Beta strandi1117 – 11237Combined sources
Beta strandi1129 – 11346Combined sources
Beta strandi1142 – 115211Combined sources
Beta strandi1428 – 14325Combined sources
Beta strandi1442 – 14487Combined sources
Beta strandi1454 – 14574Combined sources
Turni1459 – 14624Combined sources
Beta strandi1474 – 14807Combined sources
Turni1481 – 14833Combined sources
Beta strandi1489 – 14935Combined sources
Beta strandi1503 – 151311Combined sources
Beta strandi1520 – 15289Combined sources
Helixi1532 – 15343Combined sources
Beta strandi1539 – 15435Combined sources
Beta strandi1566 – 15727Combined sources
Beta strandi1578 – 15858Combined sources
Beta strandi1591 – 160111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M1HX-ray1.56A/B/C/D1427-1602[»]
4ITCX-ray1.55A982-1154[»]
4RBMX-ray1.75A229-683[»]
4TKXX-ray1.60L229-680[»]
ProteinModelPortaliQ51817.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C25 family.Sequence Analysis

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.10390. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR011628. Cleaved_adhesin.
IPR003961. FN3_dom.
IPR001769. Gingipain.
IPR029031. Gingipain_N.
IPR018832. Pept_C25_gingipain_C.
IPR005536. Peptidase_C25_Ig-like_domain.
IPR012600. Propeptide_C25.
[Graphical view]
PfamiPF07675. Cleaved_Adhesin. 3 hits.
PF10365. DUF2436. 1 hit.
PF01364. Peptidase_C25. 1 hit.
PF03785. Peptidase_C25_C. 1 hit.
PF08126. Propeptide_C25. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q51817-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKLLLLIAA SLLGVGLYAQ SAKIKLDAPT TRTTCTNNSF KQFDASFSFN
60 70 80 90 100
EVELTKVETK GGTFASVSIP GAFPTGEVGS PEVPAVRKLI AVPVGATPVV
110 120 130 140 150
RVKSFTEQVY SLNQYGSEKL MPHQPSMSKS DDPEKVPFVY NAAAYARKGF
160 170 180 190 200
VGQELTQVEM LGTMRGVRIA ALTINPVQYD VVANQLKVRN NIEIEVSFQG
210 220 230 240 250
ADEVATQRLY DASFSPYFET AYKQLFNRDV YTDHGDLYNT PVRMLVVAGA
260 270 280 290 300
KFKEALKPWL TWKAQKGFYL DVHYTDEAEV GTTNASIKAF IHKKYNDGLA
310 320 330 340 350
ASAAPVFLAL VGDTDVISGE KGKKTKKVTD LYYSAVDGDY FPEMYTFRMS
360 370 380 390 400
ASSPEELTNI IDKVLMYEKA TMPDKSYLEK VLLIAGADYS WNSQVGQPTI
410 420 430 440 450
KYGMQYYYNQ EHGYTDVYNY LKAPYTGCYS HLNTGVSFAN YTAHGSETAW
460 470 480 490 500
ADPLLTTSQL KALTNKDKYF LAIGNCCITA QFDYVQPCFG EVITRVKEKG
510 520 530 540 550
AYAYIGSSPN SYWGEDYYWS VGANAVFGVQ PTFEGTSMGS YDATFLEDSY
560 570 580 590 600
NTVNSIMWAG NLAATHAGNI GNITHIGAHY YWEAYHVLGD GSVMPYRAMP
610 620 630 640 650
KTNTYTLPAS LPQNQASYSI QASAGSYVAI SKDGVLYGTG VANASGVATV
660 670 680 690 700
SMTKQITENG NYDVVITRSN YLPVIKQIQV GEPSPYQPVS NLTATTQGQK
710 720 730 740 750
VTLKWEAPSA KKAEGSREVK RIGDGLFVTI EPANDVRANE AKVVLAADNV
760 770 780 790 800
WGDNTGYQFL LDADHNTFGS VIPATGPLFT GTASSNLYSA NFEYLVPANA
810 820 830 840 850
DPVVTTQNII VTGQGEVVIP GGVYDYCITN PEPASGKMWI AGDGGNQPAR
860 870 880 890 900
YDDFTFEAGK KYTFTMRRAG MGDGTDMEVE DDSPASYTYT VYRDGTKIKE
910 920 930 940 950
GLTATTFEED GVAAGNHEYC VEVKYTAGVS PKVCKDVTVE GSNEFAPVQN
960 970 980 990 1000
LTGSSVGQKV TLKWDAPNGT PNPNPNPNPN PGTTLSESFE NGIPASWKTI
1010 1020 1030 1040 1050
DADGDGHGWK PGNAPGIAGY NSNGCVYSES FGLGGIGVLT PDNYLITPAL
1060 1070 1080 1090 1100
DLPNGGKLTF WVCAQDANYA SEHYAVYASS TGNDASNFTN ALLEETITAK
1110 1120 1130 1140 1150
GVRSPKAIRG RIQGTWRQKT VDLPAGTKYV AFRHFQSTDM FYIDLDEVEI
1160 1170 1180 1190 1200
KANGKRADFT ETFESSTHGE APAEWTTIDA DGDGQGWLCL SSGQLDWLTA
1210 1220 1230 1240 1250
HGGSNVVSSF SWNGMALNPD NYLISKDVTG ATKVKYYYAV NDGFPGDHYA
1260 1270 1280 1290 1300
VMISKTGTNA GDFTVVFEET PNGINKGGAR FGLSTEANGA KPQSVWIERT
1310 1320 1330 1340 1350
VDLPAGTKYV AFRHYNCSDL NYILLDDIQF TMGGSPTPTD YTYTVYRDGT
1360 1370 1380 1390 1400
KIKEGLTETT FEEDGVATGN HEYCVEVKYT AGVSPKKCVD VTVNSTQFNP
1410 1420 1430 1440 1450
VQNLTAEQAP NSMDAILKWN APASKRAEVL NEDFENGIPA SWKTIDADGD
1460 1470 1480 1490 1500
GNNWTTTPPP GGSSFAGHNS AICVSSASHI NFEGPQNPDN YLVTPELSLP
1510 1520 1530 1540 1550
GGGTLTFWVC AQDANYASEH YAVYASSTGN DASNFANALL EEVLTAKTVV
1560 1570 1580 1590 1600
TAPEAIRGTR AQGTWYQKTV QLPAGTKYVA FRHFGCTDFF WINLDDVVIT
1610 1620 1630 1640 1650
SGNAPSYTYT IYRNNTQIAS GVTETTYRDP DLATGFYTYG VKVVYPNGES
1660 1670 1680 1690 1700
AIETATLNIT SLADVTAQKP YTLTVVGKTI TVTCQGEAMI YDMNGRRLAA
1710 1720 1730
GRNTVVYTAQ GGHYAVMVVV DGKSYVEKLA VK
Length:1,732
Mass (Da):187,875
Last modified:October 31, 1996 - v1
Checksum:i654271DBEF7BCAE4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti796 – 7961V → I in AAB60809 (PubMed:10219167).Curated
Sequence conflicti1351 – 13511K → N in AAC26523 (PubMed:9632563).Curated
Sequence conflicti1364 – 13641D → Y in AAC26523 (PubMed:9632563).Curated
Sequence conflicti1390 – 13901D → N in AAB60809 (PubMed:10219167).Curated
Sequence conflicti1448 – 14481D → H in AAC26523 (PubMed:9632563).Curated
Sequence conflicti1479 – 14791H → Y in AAB60809 (PubMed:10219167).Curated

Polymorphismi

Several forms of kgp with differences at the C-terminus exist in different P.gingivalis strains.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U42210 Genomic DNA. Translation: AAB06565.1.
AF017059 Genomic DNA. Translation: AAC26523.1.
U75366 Genomic DNA. Translation: AAB60809.1.
PIRiT30836.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U42210 Genomic DNA. Translation: AAB06565.1.
AF017059 Genomic DNA. Translation: AAC26523.1.
U75366 Genomic DNA. Translation: AAB60809.1.
PIRiT30836.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M1HX-ray1.56A/B/C/D1427-1602[»]
4ITCX-ray1.55A982-1154[»]
4RBMX-ray1.75A229-683[»]
4TKXX-ray1.60L229-680[»]
ProteinModelPortaliQ51817.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC25.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.10390. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR011628. Cleaved_adhesin.
IPR003961. FN3_dom.
IPR001769. Gingipain.
IPR029031. Gingipain_N.
IPR018832. Pept_C25_gingipain_C.
IPR005536. Peptidase_C25_Ig-like_domain.
IPR012600. Propeptide_C25.
[Graphical view]
PfamiPF07675. Cleaved_Adhesin. 3 hits.
PF10365. DUF2436. 1 hit.
PF01364. Peptidase_C25. 1 hit.
PF03785. Peptidase_C25_C. 1 hit.
PF08126. Propeptide_C25. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Analysis of the prtP gene encoding porphypain, a cysteine proteinase of Porphyromonas gingivalis."
    Barkocy-Gallagher G.A., Han N., Patti J.M., Whitlock J., Progulske-Fox A., Lantz M.S.
    J. Bacteriol. 178:2734-2741(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 328-343; 738-750; 851-861; 1281-1287; 1292-1299 AND 1561-1568.
    Strain: W12Imported.
  2. "IS195, an insertion sequence-like element associated with protease genes in Porphyromonas gingivalis."
    Lewis J.P., Macrina F.L.
    Infect. Immun. 66:3035-3042(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC BAA-308 / W83Imported.
  3. "Characterization of a Porphyromonas gingivalis gene prtK that encodes a lysine-specific cysteine proteinase and three sequence-related adhesins."
    Slakeski N., Cleal S.M., Bhogal P.S., Reynolds E.C.
    Oral Microbiol. Immunol. 14:92-97(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], POST-TRANSLATIONAL PROCESSING.
    Strain: ATCC 53978 / W50Imported.
  4. "A cell-associated protein complex of Porphyromonas gingivalis W50 composed of Arg- and Lys-specific cysteine proteinases and adhesins."
    Bhogal P.S., Slakeski N., Reynolds E.C.
    Microbiology 143:2485-2495(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 229-245; 738-763; 1157-1180 AND 1292-1313.
    Strain: ATCC 53978 / W501 Publication.
  5. "Distribution of Porphyromonas gingivalis biotypes defined by alleles of the kgp (Lys-gingipain) gene."
    Nadkarni M.A., Nguyen K.A., Chapple C.C., DeCarlo A.A., Jacques N.A., Hunter N.
    J. Clin. Microbiol. 42:3873-3876(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM.

Entry informationi

Entry nameiKGP83_PORGN
AccessioniPrimary (citable) accession number: Q51817
Secondary accession number(s): O07442, O52050
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 12, 2010
Last sequence update: October 31, 1996
Last modified: March 31, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.