| IED ID | IndEnz0002018666 |
| Enzyme Type ID | protease018666 |
| Protein Name |
ATP-dependent zinc metalloprotease FtsH EC 3.4.24.- Cell division protease FtsH |
| Gene Name | ftsH BSU00690 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MNRVFRNTIFYLLILLVVIGVVSYFQTSNPKTENMSYSTFIKNLDDGKVDSVSVQPVRGVYEVKGQLKNYDKDQYFLTHVPEGKGADQIFNALKKTDVKVEPAQETSGWVTFLTTIIPFVIIFILFFFLLNQAQGGGSRVMNFGKSKAKLYTEEKKRVKFKDVAGADEEKQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPGRFDRQITVDRPDVIGREAVLKVHARNKPLDETVNLKSIAMRTPGFSGADLENLLNEAALVAARQNKKKIDARDIDEATDRVIAGPAKKSRVISKKERNIVAYHEGGHTVIGLVLDEADMVHKVTIVPRGQAGGYAVMLPREDRYFQTKPELLDKIVGLLGGRVAEEIIFGEVSTGAHNDFQRATNIARRMVTEFGMSEKLGPLQFGQSQGGQVFLGRDFNNEQNYSDQIAYEIDQEIQRIIKECYERAKQILTENRDKLELIAQTLLKVETLDAEQIKHLIDHGTLPERNFSDDEKNDDVKVNILTKTEEKKDDTKE |
| Enzyme Length | 637 |
| Uniprot Accession Number | P37476 |
| Absorption | |
| Active Site | ACT_SITE 424; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. {ECO:0000255|HAMAP-Rule:MF_01458}.; FUNCTION: In vitro partially degrades Spo0E, the phosphatase that acts on Spo0A-P. Recognition requires the last 14 residues of Spo0E (PubMed:19332814). Its stabile accumulation requires FlotA and Flot (PubMed:24222488). May degrade EzrA (Probable). {ECO:0000269|PubMed:19332814, ECO:0000269|PubMed:24222488, ECO:0000305|PubMed:24222488}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 201..208; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
| Features | Active site (1); Chain (1); Metal binding (3); Mutagenesis (2); Nucleotide binding (1); Region (1); Topological domain (3); Transmembrane (2) |
| Keywords | ATP-binding;Cell cycle;Cell division;Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Nucleotide-binding;Protease;Reference proteome;Stress response;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | INDUCTION: Induced by osmotic shock (0.8 M NaCl) and by heat shock (52 degrees Celsius). {ECO:0000269|PubMed:7608085}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:27362352, ECO:0000305|PubMed:10851010}; Multi-pass membrane protein {ECO:0000305|PubMed:10851010}; Cytoplasmic side {ECO:0000305|PubMed:10851010}. Membrane raft {ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:27362352}; Multi-pass membrane protein. Note=Accumulates in the midcell septum during vegetative cell division. At the septa colocalizes with FloA and FloT, which seem to stabilize it in the membrane (PubMed:10851010, PubMed:22882210). At the onset of sporulation appears at positions near the cell poles that may coincide with future division sites. Then, FtsH becomes concentrated at the sporulation septum and disappears from the distal pole (PubMed:10851010). Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion (PubMed:22882210, PubMed:23651456). {ECO:0000269|PubMed:10851010, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 21630458; 22512862; |
| Motif | |
| Gene Encoded By | |
| Mass | 70,937 |
| Kinetics | |
| Metal Binding | METAL 423; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 427; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 499; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
| Rhea ID | |
| Cross Reference Brenda |