| IED ID | IndEnz0002003064 |
| Enzyme Type ID | protease003064 |
| Protein Name |
ATP-dependent zinc metalloprotease FtsH EC 3.4.24.- |
| Gene Name | ftsH Acel_0159 |
| Organism | Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Acidothermales Acidothermaceae Acidothermus Acidothermus cellulolyticus Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) |
| Enzyme Sequence | MSREVTSGLPQDKPTGSAPPPPPPWRRWLLPIGLLVSLVLLFTFPMRPSSGKTLTYSEFLTALHHHDIKTITIHSDGEASGQFADGRPYSTTIPIGLAGSQLLNELENNGVQISARPPGPSLASQVLAGVLSFLPFLLLLGLFAYSGRRAGAGFLAGLPGIGRARAKIFTTERPQTRFSDVAGYDGVKAEIAEVVDFLRSPERYRRAGAAIPRGVLMVGPPGTGKTLMARAVAGEAGVPFLSVTGSSFVEMFVGVGASRVRDLFEEARKHAPCIVFVDEIDAIGQRRAGAGTIVANDEREQTLNQLLAEMDGFEPAQGVVVLAATNRPEVLDPALLRPGRFDRQVTVPLPSQADRAAILRVHCRNKRLAPDVDLDAVARATPGFSGAELANLVNEAAIAAARAGRRDLTAEDFRYARDRIILGRREDSNVLLPSERHAVAVHEAGHAVVAACSENADPVERVTILPAGRALGVTFQLPLAERHLYSESYLRDSLAVRLGGRAAELEILGEASTGAVNDLSSATELALRMVREYGLSPRLGPVSYPVGGSMYLPGGQELTPRPYAEATQQRIDQEVADLLRDAEERARDIIRRNRQAVDELASLLLEQESVDGAVVYQLVGRPVPTPEEHREAAARHVRRPGIAAATGASMAGGSEPRTAASSDDLL |
| Enzyme Length | 666 |
| Uniprot Accession Number | A0LR74 |
| Absorption | |
| Active Site | ACT_SITE 443; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
| 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. {ECO:0000255|HAMAP-Rule:MF_01458}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 219..226; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
| Features | Active site (1); Chain (1); Metal binding (3); Nucleotide binding (1); Region (2); Topological domain (3); Transmembrane (2) |
| Keywords | ATP-binding;Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Nucleotide-binding;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell 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 | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 71,287 |
| Kinetics | |
| Metal Binding | METAL 442; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 446; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 518; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
| Rhea ID | |
| Cross Reference Brenda |