| IED ID | IndEnz0002004139 |
| Enzyme Type ID | protease004139 |
| Protein Name |
Lys-gingipain HG66 EC 3.4.22.47 Cleaved into: Lys-gingipain catalytic subunit; 39 kDa adhesin; 15 kDa adhesin; 44 kDa adhesin |
| Gene Name | kgp |
| Organism | Porphyromonas gingivalis |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Porphyromonadaceae Porphyromonas Porphyromonas gingivalis |
| Enzyme Sequence | MRKLLLLIAASLLGVGLYAQNAKIKLDAPTTRTTCTNNSFKQFDASFSFNEVELTKVETKGGTFASVSIPGAFPTGEVGSPEVPAVRKLIAVPVGATPVVRVKSFTEQVYSLNQYGSEKLMPHQPSMSKSDDPEKVPFAYNAAAYARKGFVGQELTQVEMLGTMRGVRIAALTINPVQYDVVANQLKVRNNIEIEVSFQGADEVATQRLYDASFSPYFETAYKQLFNRDVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEAEVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGEKGKKTKKVTDLYYSAVDGDYFPEMYTFRMSASSPEELTNIIDKVLMYEKATMPDKSYLEKALLIAGADSYWNPKIGQQTIKYAVQYYYNQDHGYTDVYSYPKAPYTGCYSHLNTGVGFANYTAHGSETSWADPSVTATQVKALTNKNKYFLAIGNCCVTAQFDYPQPCFGEVMTRVKEKGAYAYIGSSPNSYWGEDYYWSVGANAVFGVQPTFEGTSMGSYDATFLEDSYNTVNSIMWAGNLAATHAENIGNVTHIGAHYYWEAYHVLGDGSVMPYRAMPKTNTYTLPASLPQNQASYSIQASAGSYVAISKDGVLYGTGVANASGVATVNMTKQITENGNYDVVITRSNYLPVIKQIQAGEPSPYQPVSNLTATTQGQKVTLKWDAPSAKKAEGSREVKRIGDGLFVTIEPANDVRANEAKVVLAADNVWGDNTGYQFLLDADHNTFGSVIPATGPLFTGTASSNLYSANFEYLIPANADPVVTTQNIIVTGQGEVVIPGGVYDYCITNPEPASGKMWIAGDGGNQPARYDDFTFEAGKKYTFTMRRAGMGDGTDMEVEDDSPASYTYTVYRDGTKIKEGLTATTFEEDGVAAGNHEYCVEVKYTAGVSPKVCKDVTVEGSNEFAPVQNLTGSAVGQKVTLKWDAPNGTPNPNPNPNPGTTTLSESFENGIPASWKTIDADGDGHGWKPGNAPGIAGYNSNGCVYSESFGLGGIGVLTPDNYLITPALDLPNGGKLTFWVCAQDANYASEHYAVYASSTGNDASNFTNALLEETITAKGVRSPEAIRGRIQGTWRQKTVDLPAGTKYVAFRHFQSTDMFYIDLDEVEIKANGKRADFTETFESSTHGEAPAEWTTIDADGDGQGWLCLSSGQLDWLTAHGGTNVVASFSWNGMALNPDNYLISKDVTGATKVKYYYAVNDGFPGDHYAVMISKTGTNAGDFTVVFEETPNGINKGGARFGLSTEADGAKPQSVWIERTVDLPAGTKYVAFRHYNCSDLNYILLDDIQFTMGGSPTPTDYTYTVYRDGTKIKEGLTETTFEEDGVATGNHEYCVEVKYTAGVSPKKCVNVTINPTQFNPVKNLKAQPDGGDVVLKWEAPSAKKAEGSREVKRIGDGLFVTIEPANDVRANEAKVVLAADNVWGDNTGYQFLLDADHNTFGSVIPATGPLFTGTASSNLYSANFEYLIPANADPVVTTQNIIVTGQGEVVIPGGVYDYCITNPEPASGKMWIAGDGGNQPARYDDFTFEAGKKYTFTMRRAGMGDGTDMEVEDDSPASYTYTVYRDGTKIKEGLTETTYRDAGMSAQSHEYCVEVKYAAGVSPKVCVDYIPDGVADVTAQKPYTLTVVGKTITVTCQGEAMIYDMNGRRLAAGRNTVVYTAQGGYYAVMVVVDGKSYVEKLAVK |
| Enzyme Length | 1723 |
| Uniprot Accession Number | P72197 |
| Absorption | |
| Active Site | ACT_SITE 444; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P95493; ACT_SITE 477; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P95493 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endopeptidase with strict specificity for lysyl bonds.; EC=3.4.22.47; Evidence={ECO:0000269|PubMed:8999833}; |
| DNA Binding | |
| EC Number | 3.4.22.47 |
| Enzyme Function | FUNCTION: Cysteine proteinase with a strong preference for substrates with Lys in the P1 position (PubMed:8999833). 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). {ECO:0000250|UniProtKB:B2RLK2, ECO:0000269|PubMed:8999833}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (5); Metal binding (18); Propeptide (1); Region (1); Signal peptide (1); Site (4) |
| Keywords | Calcium;Hydrolase;Metal-binding;Protease;Secreted;Signal;Thiol protease;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Lys-gingipain catalytic subunit]: Secreted {ECO:0000269|PubMed:8999833}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved into a catalytic subunit and three adhesins. Arg-gingipain is involved in this post-translational processing (By similarity). {ECO:0000250|UniProtKB:P72194, ECO:0000250|UniProtKB:Q51817}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 186,832 |
| Kinetics | |
| Metal Binding | METAL 313; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 337; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 339; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 341; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 343; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 482; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 491; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 987; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 989; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1000; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1002; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1004; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1006; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1021; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1023; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1042; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1145; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1146; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q51817 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.37;3.4.22.47; |