| IED ID | IndEnz0013000001 |
| Enzyme Type ID | keratinase000001 |
| Protein Name |
Fervidolysin EC 3.4.21.- Keratinase Subtilisin-like serine protease |
| Gene Name | fls |
| Organism | Fervidobacterium pennivorans |
| Taxonomic Lineage | cellular organisms Bacteria Thermotogae Thermotogae Thermotogales Fervidobacteriaceae Fervidobacterium Fervidobacterium pennivorans |
| Enzyme Sequence | MRKVLLIASIVALILALFSCANPSFEPRSKAKDLASLPEIKSQGYHILFGELRDGEYTEGKILVGYNDRSEVDKIVKAVNGKVVLELPQIKVVSIKLNGMTVKQAYDKIKALALKGIRYVEPSYKRELIKPTVVKPNPDMYKIRKPGLNSTARDYGEELSNELWGLEAIGVTQQLWEEASGTNIIVAVVDTGVDGTHPDLEGQVIAGYRPAFDEELPAGTDSSYGGSHGTHVAGTIAAKKDGKGIVGVAPGAKIMPIVIFDDPALVGGNGYVGDDYVAAGIIWATDHGAKVMNHSWGGWGYSYTMKEAFDYAMEHGVVMVVSAGNNTSDSHHQYPAGYPGVIQVAALDYYGGTFRVAGFSSRSDGVSVGAPGVTILSTVPGEDSIGYEGHNENVPATNGGTYDYYQGTSMAAPHVTGVVAVLLQKFPNAKPWQIRKLLENTAFDFNGNGWDHDTGYGLVKLDAALQGPLPTQGGVEEFQVVVTDAKGNFGVPTVFVSMMRDNGSCYYAKTGPDGIARFPHIDSGTYDIFVGGPDHWDRALAPYDGESIPGGYAIALRMAEERQASFVGFGVSPDATQLNVNFNSTLQVKFSTNLSTLKDPQFVVVDPLLRGVYGRVAYARNQTYDLSLLSGQISFGIQTLLPAATDITIQGTVTLNGEDIPVYGVLKAGTTWTIIDDFGGLNLGTDSQPIYVWWTIFGQ |
| Enzyme Length | 699 |
| Uniprot Accession Number | Q93LQ6 |
| Absorption | |
| Active Site | ACT_SITE 190; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000305|PubMed:12072953"; ACT_SITE 228; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000305|PubMed:12072953"; ACT_SITE 409; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000305|PubMed:12072953" |
| Activity Regulation | ACTIVITY REGULATION: Is inhibited by phenylmethylsulfonyl fluoride and 3,4-dichloroisocoumarin. EDTA and iodoacetate (1 to 5 mM) have only little effect on the enzyme activity. {ECO:0000269|PubMed:16535379}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Protease able to degrade keratin into peptides. Is responsible for keratinolysis by F.pennivorans, which allows this bacterium to grow on native feathers. {ECO:0000269|PubMed:16535379}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius. Is active in a broad temperature range, namely, between 50 and 100 degrees Celsius. Thermostable. {ECO:0000269|PubMed:16535379}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10. Is active in a broad pH range, namely, between pH 6.0 and 10.5. {ECO:0000269|PubMed:16535379}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (43); Chain (1); Domain (1); Helix (16); Metal binding (6); Mutagenesis (1); Propeptide (1); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Autocatalytic cleavage;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:16535379}. Note=Is cell-bound, probably associated with the outer cell envelope. {ECO:0000269|PubMed:16535379}. |
| Modified Residue | |
| Post Translational Modification | PTM: Undergoes auto-proteolytic processing. Once cleaved, the propeptide can remain associated with the protease and blocks its activity. The physiological activation of fervidolysin is proposed to be achieved through the stepwise removal of the propeptide accomplished by several proteolytic cleavages that may not be autolytic. {ECO:0000269|PubMed:12072953, ECO:0000269|PubMed:14687574}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000305|PubMed:12072953 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1R6V; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 75,057 |
| Kinetics | |
| Metal Binding | METAL 157; /note="Calcium"; /evidence="ECO:0000269|PubMed:14687574, ECO:0007744|PDB:1R6V"; METAL 199; /note="Calcium"; /evidence="ECO:0000269|PubMed:14687574, ECO:0007744|PDB:1R6V"; METAL 239; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:14687574, ECO:0007744|PDB:1R6V"; METAL 241; /note="Calcium"; /evidence="ECO:0000269|PubMed:14687574, ECO:0007744|PDB:1R6V"; METAL 243; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:14687574, ECO:0007744|PDB:1R6V"; METAL 245; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:14687574, ECO:0007744|PDB:1R6V" |
| Rhea ID | |
| Cross Reference Brenda |