| IED ID | IndEnz0002018487 |
| Enzyme Type ID | protease018487 |
| Protein Name |
Gelatinase EC 3.4.24.30 Coccolysin |
| Gene Name | gelE EF_1818 |
| Organism | Enterococcus faecalis (strain ATCC 700802 / V583) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Enterococcaceae Enterococcus Enterococcus faecalis (Streptococcus faecalis) Enterococcus faecalis (strain ATCC 700802 / V583) |
| Enzyme Sequence | MMKGNKILYILGTGIFVGSSCLFSSLFVAAEEQVYSESEVSTVLSKLEKEAISEAAAEQYTVVDRKEDAWGMKHLKLEKQTEGVTVDSDNVIIHLDRNGAVTSVTGNPVDQVVKIQSVDAIGEEGVKKIIASDNPETKDLVFLAIDKRVNNEGQLFYKVRVTSSPTGDPVSLVYKVNATDGTIMEKQDLTEHVGSEVTLKNSFQVAFNVPVEKSNTGIALHGTDNTGVYHAVVDGKNNYSIIQAPSLVALNQNAVDAYTHGKFVKTYYEDHFQRHSIDDRGMPILSVVDEQHPDAYDNAFWDGKAMRYGETSTPTGKTYASSLDVVGHEMTHGVTEHTAGLEYLGQSGALNESYSDLMGYIISGASNPEIGADTQSVDRKTGIRNLQTPSKHGQPETMAQYDDRARYKGTPYYDQGGVHYNSGIINRIGYTIIQNLGIEKAQTIFYSSLVNYLTPKAQFSDARDAMLAAAKVQYGDEAASVVSAAFNSAGIGAKEDIQVNQPSESVLVNE |
| Enzyme Length | 510 |
| Uniprot Accession Number | Q833V7 |
| Absorption | |
| Active Site | ACT_SITE 329; /evidence="ECO:0000250|UniProtKB:P81177, ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 419; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P81177, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by L-leucine hydroxamate and phosphoramidon. Not inhibited by phenylmethanesulfonyl fluoride. Reversibly inactivated by straight-chain aliphatic alcohols. {ECO:0000269|PubMed:2536744}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Xaa-|-Leu, Xaa-|-Phe, Xaa-|-Tyr, Xaa-|-Ala.; EC=3.4.24.30; Evidence={ECO:0000269|PubMed:2536744, ECO:0000269|PubMed:8179636}; |
| DNA Binding | |
| EC Number | 3.4.24.30 |
| Enzyme Function | FUNCTION: Metalloprotease capable of the hydrolysis of insoluble hydrophobic substrates. Hydrolyzes azocoll and gelatin and, at a lower rate, soluble and insoluble collagens. Does not cleave short synthetic peptides. Preferentially hydrolyzes the 24-Phe-|-Phe-25 bond in the insulin B-chain, followed by the 5-His-|-Leu-6 bond. Inactivates endothelin-1, primarily by cleavage of the 5-Ser-|-Leu-6 and 16-His-|-Leu-17 bonds. Hydrolyzes the alpha chain of C3 to generate a C3b-like protein. Inhibits complement-mediated hemolysis and opsinization of bacteria. Hydrolyzes the insect antimicrobial peptide cecropin. Decreases the length of E.faecalis chains via the activation of autolysin. Degrades polymerized fibrin. {ECO:0000269|PubMed:12775699, ECO:0000269|PubMed:17261598, ECO:0000269|PubMed:18941224, ECO:0000269|PubMed:2536744, ECO:0000269|PubMed:8179636}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. Active from pH 6.0-8.0, activity decreases rapidly at more acidic pH values. Stable only above pH 5.6. {ECO:0000269|PubMed:2536744}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Erroneous initiation (3); Metal binding (5); Propeptide (1); Sequence conflict (17); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17261598}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19400795; |
| Motif | |
| Gene Encoded By | |
| Mass | 55,504 |
| Kinetics | |
| Metal Binding | METAL 324; /note="Calcium"; /evidence="ECO:0000250|UniProtKB:P81177"; METAL 328; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P81177, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 332; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P81177, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 352; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P81177, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 376; /note="Calcium"; /evidence="ECO:0000250|UniProtKB:P81177" |
| Rhea ID | |
| Cross Reference Brenda |