| IED ID | IndEnz0002003321 |
| Enzyme Type ID | protease003321 |
| Protein Name |
ATP-dependent zinc metalloprotease FtsH EC 3.4.24.- |
| Gene Name | ftsH HP_1069 |
| Organism | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Epsilonproteobacteria Campylobacterales Helicobacteraceae Helicobacter Helicobacter pylori (Campylobacter pylori) Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) |
| Enzyme Sequence | MKPTNEPKKPFFQSPIILAVLGGILLIFFLRSFNSDGSFSDNFLASSTKNVSYHEIKQLISNNEVENVSIGQTLIKASHKEGNNRVIYIAKRVPDLTLVPLLDEKKINYSGFSESNFFTDMLGWLMPILVILGLWMFMANRMQKNMGGGIFGMGSAKKLINAEKPNVRFNDMAGNEEAKEEVVEIVDFLKYPERYANLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAHVPFFSMGGSSFIEMFVGLGASRVRDLFETAKKQAPSIIFIDEIDAIGKSRAAGGVVSGNDEREQTLNQLLAEMDGFGSENAPVIVLAATNRPEILDPALMRPGRFDRQVLVDKPDFNGRVEILKVHIKGVKLANDVNLQEVAKLTAGLAGADLANIINEAALLAGRNNQKEVRQQHLKEAVERGIAGLEKKSRRISPKEKKIVAYHESGHAVISEMTKGSARVNKVSIIPRGMAALGYTLNTPEENKYLMQKHELIAEIDVLLGGRAAEDVFLEEISTGASNDLERATDIIKGMVSYYGMSSVSGLMVLEKQRNAFLGGGYGSSREFSEKTAEEMDLFIKNLLEERYKHVKQTLSDYREAIEIMVKELFDKEVITGERVREIISEYEVANNLESRLIPLEEQAS |
| Enzyme Length | 632 |
| Uniprot Accession Number | P71408 |
| Absorption | |
| Active Site | ACT_SITE 435; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
| Activity Regulation | |
| Binding Site | BINDING 173; /note=ATP; via amide nitrogen and carbonyl oxygen; BINDING 354; /note=ATP |
| 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}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 213..217; /note=ATP |
| Features | Active site (1); Beta strand (15); Binding site (2); Chain (1); Helix (10); Metal binding (3); Nucleotide binding (1); Sequence conflict (14); Topological domain (3); Transmembrane (2); Turn (7) |
| 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 | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:8892813}; Multi-pass membrane protein {ECO:0000305|PubMed:8892813}; Cytoplasmic side {ECO:0000305|PubMed:8892813}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2R62; 2R65; |
| Mapped Pubmed ID | 11196647; |
| Motif | |
| Gene Encoded By | |
| Mass | 69,745 |
| Kinetics | |
| Metal Binding | METAL 434; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 438; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 511; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
| Rhea ID | |
| Cross Reference Brenda |