| IED ID | IndEnz0002003317 |
| Enzyme Type ID | protease003317 |
| Protein Name |
ATP-dependent zinc metalloprotease FtsH EC 3.4.24.- Cell division protease FtsH |
| Gene Name | ftsH hflB mrsC std tolZ b3178 JW3145 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MAKNLILWLVIAVVLMSVFQSFGPSESNGRKVDYSTFLQEVNNDQVREARINGREINVTKKDSNRYTTYIPVQDPKLLDNLLTKNVKVVGEPPEEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGKGAMSFGKSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGPEHVSTGASNDIKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVFLGRSVAKAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKYETIDAPQIDDLMARRDVRPPAGWEEPGASNNSGDNGSPKAPRPVDEPRTPNPGNTMSEQLGDK |
| Enzyme Length | 644 |
| Uniprot Accession Number | P0AAI3 |
| Absorption | |
| Active Site | ACT_SITE 415; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: (Microbial infection) Activity against phage lambda cII protein is inhibited by EDTA but not by PMSF. In vitro pre-incubation of FtsH with HflKC abolishes its activity against phage lambda cII protein at the cytoplasmic side of the membrane. {ECO:0000269|PubMed:9159109}. |
| 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements. It presumably dislocates membrane-spanning and periplasmic segments of the protein into the cytoplasm to degrade them, this probably requires ATP. Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA.; FUNCTION: As FtsH regulates the levels of both LpxC and KdtA it is required for synthesis of both the protein and lipid components of lipopolysaccharide (LPS). {ECO:0000269|PubMed:18776015}.; FUNCTION: (Microbial infection) Probably transports the toxic C-terminal region of CdiA from E.coli strain 536, E.cloacae strain ATCC 13047 and of Y.pestis strain A across the inner membrane to the cytoplasm, where CdiA has a toxic effect. Toxin transport is strain-specific, mutations in this gene do not confer resistance to several other tested CdiA toxins. {ECO:0000269|PubMed:26305955}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 192..199; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
| Features | Active site (1); Beta strand (12); Chain (1); Erroneous initiation (1); Helix (15); Metal binding (3); Mutagenesis (22); Nucleotide binding (1); Region (1); Site (1); Topological domain (3); Transmembrane (2); Turn (1) |
| Keywords | 3D-structure;ATP-binding;Cell inner membrane;Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Nucleotide-binding;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc |
| Interact With | P0ABC3; P0ABC7; P0AGB3; P03042 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01458, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8444797, ECO:0000269|PubMed:8947034}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8444797, ECO:0000269|PubMed:8947034}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1LV7; 4V0B; |
| Mapped Pubmed ID | 10512625; 10809689; 15690043; 16606699; 20706981; 23166924; 25576874; |
| Motif | |
| Gene Encoded By | |
| Mass | 70,708 |
| Kinetics | |
| Metal Binding | METAL 414; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 418; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 492; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B17;3.4.24.B20; |