| IED ID | IndEnz0002005794 |
| Enzyme Type ID | protease005794 |
| Protein Name |
Gingipain R1 EC 3.4.22.37 Arg-gingipain Gingipain 1 RGP-1 |
| Gene Name | rgpA rgp1 |
| Organism | Porphyromonas gingivalis |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Porphyromonadaceae Porphyromonas Porphyromonas gingivalis |
| Enzyme Sequence | MKNLNKFVSIALCSSLLGGMAFAQQTELGRNPNVRLLESTQQSVTKVQFRMDNLKFTEVQTPKGMAQVPTYTEGVNLSEKGMPTLPILSRSLAVSDTREMKVEVVSSKFIEKKNVLIAPSKGMIMRNEDPKKIPYVYGKSYSQNKFFPGEIATLDDPFILRDVRGQVVNFAPLQYNPVTKTLRIYTEITVAVSETSEQGKNILNKKGTFAGFEDTYKRMFMNYEPGRYTPVEEKQNGRMIVIVAKKYEGDIKDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNDLTYVLLVGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDLKTQIDRTIHYERNITTEDKWLGQALCIASAEGGPSADNGESDIQHENVIANLLTQYGYTKIIKCYDPGVTPKNIIDAFNGGISLVNYTGHGSETAWGTSHFGTTHVKQLTNSNQLPFIFDVACVNGDFLFSMPCFAEALMRAQKDGKPTGTVAIIASTINQSWASPMRGQDEMNEILCEKHPNNIKRTFGGVTMNGMFAMVEKYKKDGEKMLDTWTVFGDPSLLVRTLVPTKMQVTAPAQINLTDASVNVSCDYNGAIATISANGKMFGSAVVENGTATINLTGLTNESTLTLTVVGYNKETVIKTINTNGEPNPYQPVSNLTATTQGQKVTLKWDAPSTKTNATTNTARSVDGIRELVLLSVSDAPELLRSGQAEIVLEAHDVWNDGSGYQILLDADHDQYGQVIPSDTHTLWPNCSVPANLFAPFEYTVPENADPSCSPTNMIMDGTASVNIPAGTYDFAIAAPQANAKIWIAGQGPTKEDDYVFEAGKKYHFLMKKMGSGDGTELTISEGGGSDYTYTVYRDGTKIKEGLTETTYRDAGMSAQSHEYCVEVKYAAGVSPKVCVDYIPDGVADVTAQKPYTLTVVGKTITVTCQGEAMIYDMNGRRLAAGRNTVVYTAQGGYYAVMVVVDGKSYVEKLAVK |
| Enzyme Length | 991 |
| Uniprot Accession Number | P28784 |
| Absorption | |
| Active Site | ACT_SITE 438; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 471; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P95493 |
| Activity Regulation | ACTIVITY REGULATION: Requires cysteine for activation and Ca(2+) and/or Mg(2+) for stabilization. It is stimulated by glycine-containing dipeptides. It is resistant to inhibition by proteinase inhibitors in human plasma. {ECO:0000269|PubMed:1527017}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1.; EC=3.4.22.37; Evidence={ECO:0000269|PubMed:1527017}; |
| DNA Binding | |
| EC Number | 3.4.22.37 |
| Enzyme Function | FUNCTION: Thiol protease. Acts synergistically with RgpB to catalyze the maturation of fimbrial subunits, such as FimA (By similarity). Its proteolytic activity is a major factor in both periodontal tissue destruction and in evasion of host defense mechanisms (Probable). {ECO:0000250|UniProtKB:B2RKU0, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (13); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Secreted;Signal;Thiol protease;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1527017, ECO:0000269|PubMed:7864651}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 108,782 |
| Kinetics | |
| Metal Binding | METAL 305; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P95493; METAL 327; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P95493; METAL 330; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P95493; METAL 332; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P95493; METAL 334; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P95493; METAL 388; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P95493; METAL 393; /note=Calcium 3; via pros nitrogen; /evidence=ECO:0000250|UniProtKB:P95493; METAL 476; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P95493; METAL 485; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P95493; METAL 519; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P95493; METAL 520; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:P95493; METAL 523; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:P95493; METAL 529; /note=Calcium 4; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P95493 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.37; |