IED ID | IndEnz0002004335 |
Enzyme Type ID | protease004335 |
Protein Name |
ATP-dependent zinc metalloprotease FtsH EC 3.4.24.- |
Gene Name | ftsH CTL0213 |
Organism | Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) |
Taxonomic Lineage | cellular organisms Bacteria PVC group Chlamydiae Chlamydiia Chlamydiales Chlamydiaceae Chlamydia/Chlamydophila group Chlamydia Chlamydia trachomatis Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) |
Enzyme Sequence | MAKDKKTNPESKKSFPTAFFFLLFGVIFGVVTVQNFFSAKKASVGFSHQLEHLVNLKLLIPEESRKTALNDNLVSFSGRFREVVPAEGQVRYQYLDLIERKHQIDFELEEASKSLTVLSKEVRNAITWFSAISGMPIPEAGYTISPRTDVGLSVLEPLVVYGPVDAQIVNLAALENRVRSLPKSTESLRVFGSDLYALIGKYLSPALGIGSESLKKEIKDLHQQVENSLTQVIEGDQAVALYKTVLETLHRISLALVSPEEGTRFHQLRSVRLYREDFNRCVKLLRESDETQVQLDKLRGELVQAVWYFNNQELSSRALEKQDPEVFSRWFEGAKQEWAAFSSNKSLSFRAPDQPRNLVLEKTFRSEEPTPHYSGYLFTFMPIILVLLFIYFIFSRQVKGMNGSAMSFGKSPARLLAKGQNKVTFADVAGIEEAKEELVEIVDFLKNPTKFTSLGGRIPKGILLIGAPGTGKTLIAKAVAGEADRPFFSIAGSDFVEMFVGVGASRIRDMFEQAKRNAPCIIFIDEIDAVGRHRGAGIGGGHDEREQTLNQLLVEMDGFGTNEGVILMAATNRPDVLDKALLRPGRFDRRVVVNLPDIKGRFEILAVHAKRIKLDPTVDLMAVARSTPGASGADLENLLNEAALLAARKDRTAVTAVEVAEARDKVLYGKERRSLEMDAQEKKTTAYHESGHAIVGLCVEHSDPVDKVTIIPRGLSLGATHFLPEKNKLSYWKKELYDQLAVLMGGRAAEQIFLGDVSSGAQQDIAQATKIVRSMICEWGMSDHLGTVAYDEHSEAAPTGYGSYHEKNYSEETAKVIDNELKTLLDAAYQRALDIINSHKEELELMTQMLIEFETLDSKDVKEIMDHSWDADKKRARMKEEGMLYKKISEDLPPPPPQENVQDGTSLKFNTST |
Enzyme Length | 913 |
Uniprot Accession Number | B0B970 |
Absorption | |
Active Site | ACT_SITE 689; /evidence=ECO:0000250 |
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 (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | NP_BIND 466..473; /note=ATP; /evidence=ECO:0000255 |
Features | Active site (1); Chain (1); Metal binding (3); Nucleotide binding (1); Region (3); Topological domain (3); Transmembrane (2) |
Keywords | ATP-binding;Cell inner membrane;Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Nucleotide-binding;Protease;Transmembrane;Transmembrane helix;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 101,815 |
Kinetics | |
Metal Binding | METAL 688; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 692; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 764; /note=Zinc; catalytic; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |