Detail Information for IndEnz0002018487
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