IED Industry Enzyme Database

Detail Information for IndEnz0002002723
IED ID IndEnz0002002723
Enzyme Type ID protease002723
Protein Name Lys-gingipain W83
EC 3.4.22.47
Lysine specific cysteine protease
Lysine-specific cysteine proteinase
Porphypain
PrtK48

Cleaved into: Lys-gingipain catalytic subunit; 39 kDa adhesin
PrtK39
; 15 kDa adhesin
PrtK15
; 44 kDa adhesin
PrtK44
Gene Name kgp prtK prtP
Organism Porphyromonas gingivalis
Taxonomic Lineage cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Porphyromonadaceae Porphyromonas Porphyromonas gingivalis
Enzyme Sequence MRKLLLLIAASLLGVGLYAQSAKIKLDAPTTRTTCTNNSFKQFDASFSFNEVELTKVETKGGTFASVSIPGAFPTGEVGSPEVPAVRKLIAVPVGATPVVRVKSFTEQVYSLNQYGSEKLMPHQPSMSKSDDPEKVPFVYNAAAYARKGFVGQELTQVEMLGTMRGVRIAALTINPVQYDVVANQLKVRNNIEIEVSFQGADEVATQRLYDASFSPYFETAYKQLFNRDVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEAEVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGEKGKKTKKVTDLYYSAVDGDYFPEMYTFRMSASSPEELTNIIDKVLMYEKATMPDKSYLEKVLLIAGADYSWNSQVGQPTIKYGMQYYYNQEHGYTDVYNYLKAPYTGCYSHLNTGVSFANYTAHGSETAWADPLLTTSQLKALTNKDKYFLAIGNCCITAQFDYVQPCFGEVITRVKEKGAYAYIGSSPNSYWGEDYYWSVGANAVFGVQPTFEGTSMGSYDATFLEDSYNTVNSIMWAGNLAATHAGNIGNITHIGAHYYWEAYHVLGDGSVMPYRAMPKTNTYTLPASLPQNQASYSIQASAGSYVAISKDGVLYGTGVANASGVATVSMTKQITENGNYDVVITRSNYLPVIKQIQVGEPSPYQPVSNLTATTQGQKVTLKWEAPSAKKAEGSREVKRIGDGLFVTIEPANDVRANEAKVVLAADNVWGDNTGYQFLLDADHNTFGSVIPATGPLFTGTASSNLYSANFEYLVPANADPVVTTQNIIVTGQGEVVIPGGVYDYCITNPEPASGKMWIAGDGGNQPARYDDFTFEAGKKYTFTMRRAGMGDGTDMEVEDDSPASYTYTVYRDGTKIKEGLTATTFEEDGVAAGNHEYCVEVKYTAGVSPKVCKDVTVEGSNEFAPVQNLTGSSVGQKVTLKWDAPNGTPNPNPNPNPNPGTTLSESFENGIPASWKTIDADGDGHGWKPGNAPGIAGYNSNGCVYSESFGLGGIGVLTPDNYLITPALDLPNGGKLTFWVCAQDANYASEHYAVYASSTGNDASNFTNALLEETITAKGVRSPKAIRGRIQGTWRQKTVDLPAGTKYVAFRHFQSTDMFYIDLDEVEIKANGKRADFTETFESSTHGEAPAEWTTIDADGDGQGWLCLSSGQLDWLTAHGGSNVVSSFSWNGMALNPDNYLISKDVTGATKVKYYYAVNDGFPGDHYAVMISKTGTNAGDFTVVFEETPNGINKGGARFGLSTEANGAKPQSVWIERTVDLPAGTKYVAFRHYNCSDLNYILLDDIQFTMGGSPTPTDYTYTVYRDGTKIKEGLTETTFEEDGVATGNHEYCVEVKYTAGVSPKKCVDVTVNSTQFNPVQNLTAEQAPNSMDAILKWNAPASKRAEVLNEDFENGIPASWKTIDADGDGNNWTTTPPPGGSSFAGHNSAICVSSASHINFEGPQNPDNYLVTPELSLPGGGTLTFWVCAQDANYASEHYAVYASSTGNDASNFANALLEEVLTAKTVVTAPEAIRGTRAQGTWYQKTVQLPAGTKYVAFRHFGCTDFFWINLDDVVITSGNAPSYTYTIYRNNTQIASGVTETTYRDPDLATGFYTYGVKVVYPNGESAIETATLNITSLADVTAQKPYTLTVVGKTITVTCQGEAMIYDMNGRRLAAGRNTVVYTAQGGHYAVMVVVDGKSYVEKLAVK
Enzyme Length 1732
Uniprot Accession Number Q51817
Absorption
Active Site ACT_SITE 444; /note=Proton donor; /evidence=ECO:0000305|PubMed:25266723; ACT_SITE 477; /note=Nucleophile; /evidence=ECO:0000269|PubMed:25266723
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:9245829};
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 (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). {ECO:0000250|UniProtKB:B2RLK2, ECO:0000269|PubMed:24265933, ECO:0000269|PubMed:9245829}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (55); Chain (5); Helix (21); Metal binding (28); Propeptide (1); Region (1); Sequence conflict (6); Signal peptide (1); Site (4); Turn (12)
Keywords 3D-structure;Calcium;Direct protein sequencing;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:9245829}.; SUBCELLULAR LOCATION: [39 kDa adhesin]: Secreted {ECO:0000269|PubMed:9245829}.; SUBCELLULAR LOCATION: [15 kDa adhesin]: Secreted {ECO:0000269|PubMed:9245829}.; SUBCELLULAR LOCATION: [44 kDa adhesin]: Secreted {ECO:0000269|PubMed:9245829}.
Modified Residue
Post Translational Modification PTM: Proteolytically cleaved into a catalytic subunit and three adhesins. Arg-gingipain is involved in this post-translational processing. {ECO:0000269|PubMed:9245829}.
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000255
Structure 3D X-ray crystallography (6)
Cross Reference PDB 3M1H; 4ITC; 4RBM; 4TKX; 5MUN; 6I9A;
Mapped Pubmed ID 28196869; 30894633;
Motif
Gene Encoded By
Mass 187,875
Kinetics
Metal Binding METAL 313; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:25266723, ECO:0007744|PDB:4RBM"; METAL 337; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:25266723, ECO:0007744|PDB:4RBM"; METAL 339; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:25266723, ECO:0007744|PDB:4RBM"; METAL 341; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:25266723, ECO:0007744|PDB:4RBM"; METAL 343; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:25266723, ECO:0007744|PDB:4RBM"; METAL 482; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:25266723, ECO:0007744|PDB:4RBM"; METAL 491; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:25266723, ECO:0007744|PDB:4RBM"; METAL 988; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:24265933, ECO:0007744|PDB:4ITC"; METAL 990; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:24265933, ECO:0007744|PDB:4ITC"; METAL 1001; /note="Calcium 4"; /evidence="ECO:0000269|PubMed:24265933, ECO:0007744|PDB:4ITC"; METAL 1003; /note="Calcium 4"; /evidence="ECO:0000269|PubMed:24265933, ECO:0007744|PDB:4ITC"; METAL 1005; /note="Calcium 4"; /evidence="ECO:0000269|PubMed:24265933, ECO:0007744|PDB:4ITC"; METAL 1007; /note="Calcium 4; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:24265933, ECO:0007744|PDB:4ITC"; METAL 1022; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:24265933, ECO:0007744|PDB:4ITC"; METAL 1024; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:24265933, ECO:0007744|PDB:4ITC"; METAL 1043; /note="Calcium 4"; /evidence="ECO:0000269|PubMed:24265933, ECO:0007744|PDB:4ITC"; METAL 1146; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:24265933, ECO:0007744|PDB:4ITC"; METAL 1147; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:24265933, ECO:0007744|PDB:4ITC"; METAL 1433; /note="Calcium 5; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:21812842, ECO:0007744|PDB:3M1H"; METAL 1435; /note="Calcium 5"; /evidence="ECO:0000269|PubMed:21812842, ECO:0007744|PDB:3M1H"; METAL 1446; /note="Calcium 6"; /evidence="ECO:0000269|PubMed:21812842, ECO:0007744|PDB:3M1H"; METAL 1448; /note="Calcium 6"; /evidence="ECO:0000269|PubMed:21812842, ECO:0007744|PDB:3M1H"; METAL 1450; /note="Calcium 6"; /evidence="ECO:0000269|PubMed:21812842, ECO:0007744|PDB:3M1H"; METAL 1452; /note="Calcium 6; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:21812842, ECO:0007744|PDB:3M1H"; METAL 1470; /note="Calcium 5"; /evidence="ECO:0000269|PubMed:21812842, ECO:0007744|PDB:3M1H"; METAL 1472; /note="Calcium 5; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:21812842, ECO:0007744|PDB:3M1H"; METAL 1490; /note="Calcium 6"; /evidence="ECO:0000269|PubMed:21812842, ECO:0007744|PDB:3M1H"; METAL 1595; /note="Calcium 5"; /evidence="ECO:0000269|PubMed:21812842, ECO:0007744|PDB:3M1H"
Rhea ID
Cross Reference Brenda 3.4.22.47;