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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 (PubMed:9245829). 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). Has hemolytic activity; this is mediated by the adhesin domains and does not require the catalytic domain (PubMed:21812842, PubMed:24265933).By similarity2 Publications

Catalytic activityi

Endopeptidase with strict specificity for lysyl bonds.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi313Calcium 1Combined sources1 Publication1
Metal bindingi337Calcium 2Combined sources1 Publication1
Metal bindingi339Calcium 2Combined sources1 Publication1
Metal bindingi341Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi343Calcium 2Combined sources1 Publication1
Active sitei444Proton donor1 Publication1
Active sitei477Nucleophile1 Publication1
Metal bindingi482Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi491Calcium 1Combined sources1 Publication1
Metal bindingi988Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi990Calcium 3Combined sources1 Publication1
Metal bindingi1001Calcium 4Combined sources1 Publication1
Metal bindingi1003Calcium 4Combined sources1 Publication1
Metal bindingi1005Calcium 4Combined sources1 Publication1
Metal bindingi1007Calcium 4; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1022Calcium 3Combined sources1 Publication1
Metal bindingi1024Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1043Calcium 4Combined sources1 Publication1
Metal bindingi1146Calcium 3Combined sources1 Publication1
Metal bindingi1147Calcium 3Combined sources1 Publication1
Metal bindingi1433Calcium 5; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1435Calcium 5Combined sources1 Publication1
Metal bindingi1446Calcium 6Combined sources1 Publication1
Metal bindingi1448Calcium 6Combined sources1 Publication1
Metal bindingi1450Calcium 6Combined sources1 Publication1
Metal bindingi1452Calcium 6; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1470Calcium 5Combined sources1 Publication1
Metal bindingi1472Calcium 5; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi1490Calcium 6Combined sources1 Publication1
Metal bindingi1595Calcium 5Combined sources1 Publication1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • cysteine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • hemolysis in other organism Source: UniProtKB
  • pathogenesis Source: UniProtKB-KW
  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Virulence

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

MEROPSiC25.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Lys-gingipain W831 PublicationBy similarity (EC:3.4.22.471 Publication)
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

Lys-gingipain catalytic subunit :
39 kDa adhesin :
15 kDa adhesin :
44 kDa adhesin :

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000039538125 – 2281 PublicationAdd BLAST204
ChainiPRO_0000395382229 – 1732Lys-gingipain W831 PublicationAdd BLAST1504
ChainiPRO_0000395383229 – 680Lys-gingipain catalytic subunit2 PublicationsAdd BLAST452
ChainiPRO_0000395384738 – ?39 kDa adhesin1 Publication
ChainiPRO_00003953851157 – ?15 kDa adhesin1 Publication
ChainiPRO_00003953861292 – ?44 kDa adhesin2 Publications

Post-translational modificationi

Proteolytically cleaved into a catalytic subunit and three adhesins. Arg-gingipain is involved in this post-translational processing.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei228 – 229Cleavage; site 11 Publication2
Sitei737 – 738Cleavage; site 21 Publication2
Sitei1156 – 1157Cleavage; site 31 Publication2
Sitei1291 – 1292Cleavage; site 41 Publication2

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiQ51817.

Structurei

Secondary structure

11732
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi230 – 233Combined sources4
Beta strandi240 – 248Combined sources9
Helixi250 – 252Combined sources3
Helixi253 – 265Combined sources13
Beta strandi268 – 274Combined sources7
Turni278 – 280Combined sources3
Helixi284 – 300Combined sources17
Beta strandi306 – 312Combined sources7
Turni314 – 316Combined sources3
Turni323 – 325Combined sources3
Beta strandi327 – 330Combined sources4
Helixi331 – 334Combined sources4
Beta strandi337 – 341Combined sources5
Beta strandi343 – 349Combined sources7
Helixi354 – 369Combined sources16
Helixi375 – 379Combined sources5
Beta strandi380 – 385Combined sources6
Helixi391 – 394Combined sources4
Helixi396 – 406Combined sources11
Helixi410 – 412Combined sources3
Beta strandi415 – 420Combined sources6
Turni426 – 429Combined sources4
Helixi430 – 434Combined sources5
Beta strandi437 – 443Combined sources7
Turni451 – 454Combined sources4
Helixi457 – 461Combined sources5
Beta strandi470 – 478Combined sources9
Beta strandi484 – 486Combined sources3
Helixi489 – 495Combined sources7
Beta strandi499 – 509Combined sources11
Helixi513 – 521Combined sources9
Turni533 – 535Combined sources3
Helixi540 – 545Combined sources6
Beta strandi547 – 549Combined sources3
Helixi553 – 569Combined sources17
Helixi578 – 584Combined sources7
Beta strandi585 – 589Combined sources5
Beta strandi616 – 622Combined sources7
Beta strandi627 – 632Combined sources6
Beta strandi635 – 642Combined sources8
Beta strandi646 – 654Combined sources9
Beta strandi660 – 667Combined sources8
Beta strandi674 – 680Combined sources7
Beta strandi984 – 987Combined sources4
Beta strandi997 – 1001Combined sources5
Beta strandi1010 – 1013Combined sources4
Turni1014 – 1016Combined sources3
Beta strandi1022 – 1032Combined sources11
Turni1033 – 1036Combined sources4
Beta strandi1043 – 1046Combined sources4
Beta strandi1056 – 1066Combined sources11
Beta strandi1073 – 1081Combined sources9
Helixi1085 – 1087Combined sources3
Beta strandi1090 – 1096Combined sources7
Beta strandi1117 – 1123Combined sources7
Beta strandi1129 – 1134Combined sources6
Beta strandi1142 – 1152Combined sources11
Beta strandi1428 – 1432Combined sources5
Beta strandi1442 – 1448Combined sources7
Beta strandi1454 – 1457Combined sources4
Turni1459 – 1462Combined sources4
Beta strandi1474 – 1480Combined sources7
Turni1481 – 1483Combined sources3
Beta strandi1489 – 1493Combined sources5
Beta strandi1503 – 1513Combined sources11
Beta strandi1520 – 1528Combined sources9
Helixi1532 – 1534Combined sources3
Beta strandi1539 – 1543Combined sources5
Beta strandi1566 – 1572Combined sources7
Beta strandi1578 – 1585Combined sources8
Beta strandi1591 – 1601Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3M1HX-ray1.56A/B/C/D1427-1602[»]
4ITCX-ray1.55A982-1154[»]
4RBMX-ray1.75A229-683[»]
4TKXX-ray1.60L229-680[»]
ProteinModelPortaliQ51817.
SMRiQ51817.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The isolated adhesin domains have hemolytic activity (in vitro).2 Publications

Sequence similaritiesi

Belongs to the peptidase C25 family.Sequence analysis

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.40.50.10390. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR011628. Cleaved_adhesin.
IPR001769. Gingipain.
IPR029031. Gingipain_N.
IPR013783. Ig-like_fold.
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]
SUPFAMiSSF52129. SSF52129. 1 hit.

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:November 1, 1996 - v1
Checksum:i654271DBEF7BCAE4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti796V → I in AAB60809 (PubMed:10219167).Curated1
Sequence conflicti1351K → N in AAC26523 (PubMed:9632563).Curated1
Sequence conflicti1364D → Y in AAC26523 (PubMed:9632563).Curated1
Sequence conflicti1390D → N in AAB60809 (PubMed:10219167).Curated1
Sequence conflicti1448D → H in AAC26523 (PubMed:9632563).Curated1
Sequence conflicti1479H → Y in AAB60809 (PubMed:10219167).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3M1HX-ray1.56A/B/C/D1427-1602[»]
4ITCX-ray1.55A982-1154[»]
4RBMX-ray1.75A229-683[»]
4TKXX-ray1.60L229-680[»]
ProteinModelPortaliQ51817.
SMRiQ51817.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC25.002.

Proteomic databases

PRIDEiQ51817.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.40.50.10390. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
IPR011628. Cleaved_adhesin.
IPR001769. Gingipain.
IPR029031. Gingipain_N.
IPR013783. Ig-like_fold.
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]
SUPFAMiSSF52129. SSF52129. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKGP83_PORGN
AccessioniPrimary (citable) accession number: Q51817
Secondary accession number(s): O07442, O52050
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 75 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

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 one 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.