IED ID | IndEnz0002003037 |
Enzyme Type ID | protease003037 |
Protein Name |
Preflagellin peptidase PFP EC 3.4.23.52 |
Gene Name | flaK |
Organism | Methanococcus voltae |
Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Methanomada group Methanococci Methanococcales Methanococcaceae Methanococcus Methanococcus voltae |
Enzyme Sequence | MIAYAIGLLGLLIASIQDIKSREIENYIWIGMAVIGLLLSTYLSFTTGNFMPIISSISGFIICFIIGYLMFVLGIGGADGKILMGMGALIPSYAFPVYSSLQPLYTMEYIPWFPLLVFFNGVILMIVLPIYLFFKNLSNGVKPKKLKEYVLMLVGEYITVAEAKKGNKVVLGKGKDVKLIPSVNDDKNYDLSKYKDTQYVWATPELPLLVPIALSYIITPFLGDKILSIILPM |
Enzyme Length | 233 |
Uniprot Accession Number | Q8NKW5 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleaves the signal peptide of 3 to 12 amino acids from the N-terminal of preflagellin, usually at Arg-Gly-|- or Lys-Gly-|-, to release flagellin.; EC=3.4.23.52; Evidence={ECO:0000269|PubMed:10633127, ECO:0000269|PubMed:14622420}; |
DNA Binding | |
EC Number | 3.4.23.52 |
Enzyme Function | FUNCTION: Cleaves the N-terminal leader peptide from preflagellins. The processing of preflagellins is necessary for assembly of flagellins into a flagellum structure. {ECO:0000269|PubMed:10633127, ECO:0000269|PubMed:14622420}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:10633127}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:10633127}; |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Mutagenesis (6); Site (2); Topological domain (7); Transmembrane (6) |
Keywords | Archaeal flagellum biogenesis;Cell membrane;Hydrolase;Membrane;Protease;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10633127}; Multi-pass membrane protein {ECO:0000269|PubMed:10633127}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 25,888 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.23.52; |