IED ID | IndEnz0002003107 |
Enzyme Type ID | protease003107 |
Protein Name |
ATP-dependent zinc metalloprotease FtsH EC 3.4.24.- |
Gene Name | ftsH TTHA1492 |
Organism | Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Deinococcus-Thermus Deinococci Thermales Thermaceae Thermus Thermus thermophilus Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) |
Enzyme Sequence | MPRAPFSLLALVLGLAFLAWAFSLAGTVGAPSGTVNYTTFLEDLKAGRVKEVVVRAGDTRIQGVLEDGSAFTTYAASPPDNATLEGWMARGVSVRVEPPQGQNALGFLWPLLLVGLLIGALYYFSRNGRAGPSDSAFSFTKSRARVLTEAPKVTFKDVAGAEEAKEELKEIVEFLKNPSRFHEMGARIPKGVLLVGPPGVGKTHLARAVAGEARVPFITASGSDFVEMFVGVGAARVRDLFETAKRHAPCIVFIDEIDAVGRKRGSGVGGGNDEREQTLNQLLVEMDGFEKDTAIVVMAATNRPDILDPALLRPGRFDRQIAIDAPDVKGREQILRIHARGKPLAEDVDLALLAKRTPGFVGADLENLLNEAALLAAREGRRKITMKDLEEAADRVMMGPAKKSLVLSPRDRRITAYHEAGHALAAHFLEHADGVHKVTIVPRGRALGFMMPRREDMLHWSRKRLLDQIAVALAGRAAEEIVFDDVTTGAENDFRQATELARRMITEWGMHPEFGPVAYAVREDTYLGGYDVRQYSEETAKRIDEAVRRLIEEQYQRVKALLLEKREVLERVAETLLERETLTAEEFQRVVEGLPLEAPEEAREEREPPRVVPKVKPGGALGGA |
Enzyme Length | 624 |
Uniprot Accession Number | Q5SI82 |
Absorption | |
Active Site | ACT_SITE 419; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
Activity Regulation | ACTIVITY REGULATION: The proteolytic activity is dependent on ATP, both the ATPase and protease activities are inhibited by ADP. {ECO:0000269|PubMed:10788805}. |
Binding Site | BINDING 159; /note=ATP; via amide nitrogen and carbonyl oxygen; BINDING 204; /note=ATP; via amide nitrogen |
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: Degrades preferentially unfolded substrates in a processive, ATP-dependent manner, usually after hydrophobic residues. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | NP_BIND 199..203; /note=ATP |
Features | Active site (1); Beta strand (8); Binding site (2); Chain (1); Compositional bias (1); Helix (14); Metal binding (3); Mutagenesis (1); Nucleotide binding (1); Region (1); Sequence conflict (2); 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 | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:10788805}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01458}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (6) |
Cross Reference PDB | 1IXZ; 1IY0; 1IY1; 1IY2; 2DHR; 4EIW; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 68,452 |
Kinetics | |
Metal Binding | METAL 418; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 422; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 493; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
Rhea ID | |
Cross Reference Brenda | 3.4.24.B17; |