| IED ID | IndEnz0002005016 |
| Enzyme Type ID | protease005016 |
| Protein Name |
Lys-gingipain EC 3.4.22.47 Lysine-specific cysteine proteinase Kgp Cleaved into: Lys-gingipain catalytic subunit; 39 kDa adhesin; 15 kDa adhesin; 44 kDa adhesin |
| Gene Name | kgp PGN_1728 |
| Organism | Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Porphyromonadaceae Porphyromonas Porphyromonas gingivalis Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561) |
| Enzyme Sequence | MRKLLLLIAASLLGVGLYAQSAKIKLDAPTTRTTCTNNSFKQFDASFSFNEVELTKVETKGGTFASVSIPGAFPTGEVGSPEVPAVRKLIAVPVGATPVVRVKSFTEQVYSLNQYGSEKLMPHQPSMSKSDDPEKVPFVYNAAAYARKGFVGQELTQVEMLGTMRGVRIAALTINPVQYDVVANQLKVRNNIEIEVSFQGADEVATQRLYDASFSPYFETAYKQLFNRDVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEAEVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGEKGKKTKKVTDLYYSAVDGDYFPEMYTFRMSASSPEELTNIIDKVLMYEKATMPDKSYLEKALLIAGADSYWNPKIGQQTIKYAVQYYYNQDHGYTDVYSYPKAPYTGCYSHLNTGVGFANYTAHGSETSWADPSLTATQVKALTNKDKYFLAIGNCCVTAQFDYPQPCFGEVMTRVKEKGAYAYIGSSPNSYWGEDYYWSVGANAVFGVQPTFEGTSMGSYDATFLEDSYNTVNSIMWAGNLAATHAGNIGNITHIGAHYYWEAYHVLGDGSVMPYRAMPKTNTYTLPASLPQNQASYSIQASAGSYVAISKDGVLYGTGVANASGVATVNMTKQITENGNYDVVITRSNYLPVIKQIQAGEPSPYQPVSNLTATTQGQKVTLKWDAPSAKKAEASREVKRIGDGLFVTIEPANDVRANEAKVVLAADNVWGDNTGYQFLLDADHNTFGSVIPATGPLFTGTASSNLYSANFEYLIPANADPVVTTQNIIVTGQGEVVIPGGVYDYCITNPEPASGKMWIAGDGGNQPARYDDFTFEAGKKYTFTMRRAGMGDGTDMEVEDDSPASYTYTVYRDGTKIQEGLTATTFEEDGVAAGNHEYCVEVKYTAGVSPKVCKDVTVEGSNEFAPVQNLTGSAVGQKVTLKWDAPNGTPNPNPNPNPGTTTLSESFENGIPASWKTIDADGDGHGWKPGNAPGIAGYNSNGCVYSESFGLGGIGVLTPDNYLITPALDLPNGGKLTFWVCAQDANYASEHYAVYASSTGNDASNFTNALLEETITAKGVRSPEAIRGRIQGTWRQKTVDLPAGTKYVAFRHFQSTDMFYIDLDEVEIKANGKRADFTETFESSTHGEAPAEWTTIDADGDGQDWLCLSSGQLDWLTAHGGTNVVASFSWNGMALNPDNYLISKDVTGATKVKYYYAVNDGFPGDHYAVMISKTGTNAGDFTVVFEETPNGINKGGARFGLSTEANGAKPQSVWIERTVDLPAGTKYVAFRHYNCSDLNYILLDDIQFTMGGSPTPTDYTYTVYRDGTKIKEGLTETTFEEDGVATGNHEYCVEVKYTAGVSPKVCVNVTINPTQFNPVKNLKAQPDGGDVVLKWEAPSGKRGELLNEDFEGDAIPTGWTALDADGDGNNWDITLNEFTRGERHVLSPLRASNVAISYSSLLQGQEYLPLTPNNFLITPKVEGAKKITYKVGSPGLPQWSHDHYALCISKSGTAAADFEVIFEETMTYTQGGANLTREKDLPAGTKYVAFRHYNCTDVLGIMIDDVVITGEGEGPSYTYTVYRDGTKIQEGLTETTYRDAGMSAQSHEYCVEVKYAAGVSPKVCVDYIPDGVADVTAQKPYTLTVVGKTITVTCQGEAMIYDMNGRRLAAGRNTVVYTAQGGYYAVMVVVDGKSYVEKLAIK |
| Enzyme Length | 1723 |
| Uniprot Accession Number | B2RLK2 |
| Absorption | |
| Active Site | ACT_SITE 444; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P95493; ACT_SITE 477; /note=Nucleophile; /evidence=ECO:0000269|PubMed:18295742 |
| Activity Regulation | ACTIVITY REGULATION: Activated by the thiol-reducing agents cysteine, 2-mercaptoethanol and dithiothreitol. Inhibited by idoacetamide, idoacetic acid, leupeptin, tosyl-L-lysine and tosyl-L-phenylalanine. Not inhibited by elastatinal, chymostatin, cystatins, alpha1-antichymotrypsin or the serine protease inhibitors phenylmethylsulfonyl fluoride and diisopropylfluorophosphate. Not inhibited by metal ion chelators. Inhibited by the heavy metal ions Fe(3+), Zn(2+), Cu(2+) and Mn(2+). {ECO:0000269|PubMed:9538207}. |
| 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:18295742, ECO:0000269|PubMed:9538207}; |
| 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. 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. {ECO:0000269|PubMed:15576324, ECO:0000269|PubMed:9538207}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Only retains 40% of activity after incubation at 60 degrees Celsius for 10 minutes. {ECO:0000269|PubMed:9538207}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. Activity remains high from pH 6.5 to 9.5. Loses 60% of its activity following incubation at pH 3.5 for 5 minutes. {ECO:0000269|PubMed:9538207}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (5); Metal binding (27); Mutagenesis (3); 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:0000250|UniProtKB:P72194}. |
| 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 | 187,262 |
| 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; METAL 1430; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1432; /note=Calcium 5; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1444; /note=Calcium 6; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1446; /note=Calcium 6; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1448; /note=Calcium 6; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1450; /note=Calcium 6; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1480; /note=Calcium 5; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1495; /note=Calcium 6; /evidence=ECO:0000250|UniProtKB:Q51817; METAL 1585; /note=Calcium 5; /evidence=ECO:0000250|UniProtKB:Q51817 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.47; |