| IED ID | IndEnz0002003105 |
| Enzyme Type ID | protease003105 |
| Protein Name |
ATP-dependent zinc metalloprotease FtsH EC 3.4.24.- |
| Gene Name | ftsH TM_0580 |
| Organism | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
| Taxonomic Lineage | cellular organisms Bacteria Thermotogae Thermotogae Thermotogales Thermotogaceae Thermotoga Thermotoga maritima Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
| Enzyme Sequence | MNRSNIWNLLFTILIIVTLFWLARFFYVENSPVSKLSYTSFVQMVEDERSVVSEVVIRDDGVLRVYTKDGRVYEVDAPWAVNDSQLIEKLVSKGIKVSGERSGSSSFWINVLGTLIPTILFIVVWLFIMRSLSGRNNQAFTFTKSRATMYKPSGNKRVTFKDVGGAEEAIEELKEVVEFLKDPSKFNRIGARMPKGILLVGPPGTGKTLLARAVAGEANVPFFHISGSDFVELFVGVGAARVRDLFAQAKAHAPCIVFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFDSKEGIIVMAATNRPDILDPALLRPGRFDKKIVVDPPDMLGRKKILEIHTRNKPLAEDVNLEIIAKRTPGFVGADLENLVNEAALLAAREGRDKITMKDFEEAIDRVIAGPARKSKLISPKEKRIIAYHEAGHAVVSTVVPNGEPVHRISIIPRGYKALGYTLHLPEEDKYLVSRNELLDKLTALLGGRAAEEVVFGDVTSGAANDIERATEIARNMVCQLGMSEELGPLAWGKEEQEVFLGKEITRLRNYSEEVASKIDEEVKKIVTNCYERAKEIIRKYRKQLDNIVEILLEKETIEGDELRRILSEEFEKVVE |
| Enzyme Length | 610 |
| Uniprot Accession Number | Q9WZ49 |
| Absorption | |
| Active Site | ACT_SITE 424; /evidence="ECO:0000255|HAMAP-Rule:MF_01458, ECO:0000269|PubMed:16484367" |
| Activity Regulation | |
| Binding Site | BINDING 164; /note=ATP; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000269|PubMed:16484367; BINDING 209; /note=ATP; via amide nitrogen; /evidence=ECO:0000269|PubMed:16484367; BINDING 343; /note=ATP; /evidence=ECO:0000269|PubMed:16484367; BINDING 371; /note=ATP; /evidence=ECO:0000269|PubMed:16484367 |
| 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 204..208; /note=ATP; /evidence=ECO:0000269|PubMed:16484367 |
| Features | Active site (1); Beta strand (12); Binding site (4); Chain (1); Helix (27); Metal binding (3); Mutagenesis (2); Nucleotide binding (1); Topological domain (3); Transmembrane (2); Turn (3) |
| 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 | Itself |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01458}; 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 (5) |
| Cross Reference PDB | 2CE7; 2CEA; 3KDS; 4M8A; 4Q0F; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 68,099 |
| Kinetics | |
| Metal Binding | METAL 423; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:16484367; METAL 427; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:16484367; METAL 500; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:16484367 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B17;3.4.24.B20; |