| IED ID | IndEnz0002001986 |
| Enzyme Type ID | protease001986 |
| Protein Name |
Gingipain R2 EC 3.4.22.37 Arg-gingipain Gingipain 2 RGP-2 |
| Gene Name | rgpB prtRII rgp2 PG_0506 |
| Organism | Porphyromonas gingivalis (strain ATCC BAA-308 / W83) |
| Taxonomic Lineage | cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Bacteroidetes Bacteroidia Bacteroidales Porphyromonadaceae Porphyromonas Porphyromonas gingivalis Porphyromonas gingivalis (strain ATCC BAA-308 / W83) |
| Enzyme Sequence | MKKNFSRIVSIVAFSSLLGGMAFAQPAERGRNPQVRLLSAEQSMSKVQFRMDNLQFTGVQTSKGVAQVPTFTEGVNISEKGTPILPILSRSLAVSETRAMKVEVVSSKFIEKKDVLIAPSKGVISRAENPDQIPYVYGQSYNEDKFFPGEIATLSDPFILRDVRGQVVNFAPLQYNPVTKTLRIYTEIVVAVSETAEAGQNTISLVKNSTFTGFEDIYKSVFMNYEATRYTPVEEKENGRMIVIVPKKYEEDIEDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNDLTYVLLVGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDLKTQIDRTIHYERNITTEDKWLGQALCIASAEGGPSADNGESDIQHENIIANLLTQYGYTKIIKCYDPGVTPKNIIDAFNGGISLANYTGHGSETAWGTSHFGTTHVKQLTNSNQLPFIFDVACVNGDFLYNVPCFAEALMRAQKDGKPTGTVAIIASTINQSWASPMRGQDEMNEILCEKHPNNIKRTFGGVTMNGMFAMVEKYKKDGEKMLDTWTVFGDPSLLVRTLVPTKMQVTAPANISASAQTFEVACDYNGAIATLSDDGDMVGTAIVKDGKAIIKLNESIADETNLTLTVVGYNKVTVIKDVKVEGTSIADVANDKPYTVAVSGKTITVESPAAGLTIFDMNGRRVATAKNRMVFEAQNGVYAVRIATEGKTYTEKVIVK |
| Enzyme Length | 736 |
| Uniprot Accession Number | P95493 |
| Absorption | |
| Active Site | ACT_SITE 440; /note="Proton donor"; /evidence="ECO:0000305|PubMed:10523290, ECO:0007744|PDB:1CVR"; ACT_SITE 473; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:23558682, ECO:0000305|PubMed:10523290, ECO:0007744|PDB:1CVR" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by human histatin-3 1/24 (histatin-5). {ECO:0000269|PubMed:11179305}. |
| 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:11179305, ECO:0000269|PubMed:9705298}; |
| DNA Binding | |
| EC Number | 3.4.22.37 |
| Enzyme Function | FUNCTION: Thiol protease. Acts synergistically with RgpA 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); Beta strand (39); Chain (1); Helix (17); Metal binding (15); Propeptide (1); Sequence conflict (12); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Signal;Thiol protease;Virulence;Zymogen |
| Interact With | P15516 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9705298}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 1CVR; 4IEF; 5AG8; 5AG9; 5HFS; |
| Mapped Pubmed ID | 23499434; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,967 |
| Kinetics | |
| Metal Binding | METAL 307; /note="Calcium 1"; /evidence="ECO:0007744|PDB:1CVR"; METAL 329; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0007744|PDB:1CVR, ECO:0007744|PDB:4IEF"; METAL 332; /note="Calcium 2"; /evidence="ECO:0007744|PDB:1CVR, ECO:0007744|PDB:4IEF"; METAL 334; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0007744|PDB:1CVR, ECO:0007744|PDB:4IEF"; METAL 336; /note="Calcium 2"; /evidence="ECO:0007744|PDB:1CVR, ECO:0007744|PDB:4IEF"; METAL 390; /note="Calcium 3"; /evidence="ECO:0007744|PDB:1CVR"; METAL 395; /note="Calcium 3; via pros nitrogen"; /evidence="ECO:0007744|PDB:1CVR"; METAL 478; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0007744|PDB:1CVR"; METAL 487; /note="Calcium 1"; /evidence="ECO:0007744|PDB:1CVR"; METAL 521; /note="Calcium 3"; /evidence="ECO:0007744|PDB:1CVR"; METAL 522; /note="Calcium 4"; /evidence="ECO:0007744|PDB:1CVR"; METAL 525; /note="Calcium 4"; /evidence="ECO:0007744|PDB:1CVR"; METAL 531; /note="Calcium 4; via tele nitrogen"; /evidence="ECO:0007744|PDB:1CVR"; METAL 613; /note="Calcium 5"; /evidence="ECO:0007744|PDB:4IEF"; METAL 639; /note="Calcium 5"; /evidence="ECO:0007744|PDB:4IEF" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.37; |