| Identification |
|---|
| HMDB Protein ID
| HMDBP13412 |
| Secondary Accession Numbers
| None |
| Name
| Gelatinase |
| Synonyms
|
- Coccolysin
|
| Gene Name
| GELE |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific 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. |
| Pathways
|
|
| Reactions
| Not Available |
| GO Classification
|
| Cellular Component |
| extracellular region |
| Molecular Function |
| metal ion binding |
| metalloendopeptidase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| 510 |
| Molecular Weight
| 55503.445 |
| Theoretical pI
| 5.128 |
| Pfam Domain Function
|
|
| Signals
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| Q833V7 |
| UniProtKB/Swiss-Prot Entry Name
| GELE_ENTFA |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Paulsen IT, Banerjei L, Myers GS, Nelson KE, Seshadri R, Read TD, Fouts DE, Eisen JA, Gill SR, Heidelberg JF, Tettelin H, Dodson RJ, Umayam L, Brinkac L, Beanan M, Daugherty S, DeBoy RT, Durkin S, Kolonay J, Madupu R, Nelson W, Vamathevan J, Tran B, Upton J, Hansen T, Shetty J, Khouri H, Utterback T, Radune D, Ketchum KA, Dougherty BA, Fraser CM: Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science. 2003 Mar 28;299(5615):2071-4. [PubMed:12663927 ]
- Su YA, Sulavik MC, He P, Makinen KK, Makinen PL, Fiedler S, Wirth R, Clewell DB: Nucleotide sequence of the gelatinase gene (gelE) from Enterococcus faecalis subsp. liquefaciens. Infect Immun. 1991 Jan;59(1):415-20. doi: 10.1128/iai.59.1.415-420.1991. [PubMed:1846126 ]
- Kirimura K, Kamigaki K, Ebihara T, Ishii Y, Kanayama S, Usami S: Determination of nucleotide sequence related to the plasmid replication region in Enterococcus faecalis and its application to a new shuttle vector. J Biosci Bioeng. 1999;87(5):566-71. doi: 10.1016/s1389-1723(99)80115-7. [PubMed:16232519 ]
- Park SY, Kim KM, Lee JH, Seo SJ, Lee IH: Extracellular gelatinase of Enterococcus faecalis destroys a defense system in insect hemolymph and human serum. Infect Immun. 2007 Apr;75(4):1861-9. doi: 10.1128/IAI.01473-06. Epub 2007 Jan 29. [PubMed:17261598 ]
- Makinen PL, Clewell DB, An F, Makinen KK: Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from Streptococcus faecalis (strain 0G1-10). J Biol Chem. 1989 Feb 25;264(6):3325-34. [PubMed:2536744 ]
- Makinen PL, Makinen KK: The Enterococcus faecalis extracellular metalloendopeptidase (EC 3.4.24.30; coccolysin) inactivates human endothelin at bonds involving hydrophobic amino acid residues. Biochem Biophys Res Commun. 1994 Apr 29;200(2):981-5. doi: 10.1006/bbrc.1994.1546. [PubMed:8179636 ]
- Waters CM, Antiporta MH, Murray BE, Dunny GM: Role of the Enterococcus faecalis GelE protease in determination of cellular chain length, supernatant pheromone levels, and degradation of fibrin and misfolded surface proteins. J Bacteriol. 2003 Jun;185(12):3613-23. doi: 10.1128/JB.185.12.3613-3623.2003. [PubMed:12775699 ]
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