IED ID | IndEnz0002003311 |
Enzyme Type ID | protease003311 |
Protein Name |
ATP-dependent zinc metalloprotease FtsH EC 3.4.24.- |
Gene Name | ftsH ACL_1386 |
Organism | Acholeplasma laidlawii (strain PG-8A) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Tenericutes Mollicutes Acholeplasmatales Acholeplasmataceae Acholeplasma Acholeplasma laidlawii Acholeplasma laidlawii (strain PG-8A) |
Enzyme Sequence | MNKQQKPKRSPLRPDYLVIVIIILLAIGMYFFFTEMMAPKVKQFDEFEFIAAIESGQIATVRSEYVGGDNFNLWEVTGTFTTGNAPEGVGSYVIILYGDRLNNIQDIIITYNELNPSTPITVSFVPHVSVDFWNIISTLLLIAAPIVLVVIMFRSMSSQSNKAQDFTKNRAKLSQGRKVKFSDIAGADEEKAEMAELIDFLKNPKKYADMGARVPKGVLLVGQPGTGKTLLAKAVAGEAQVPFFSISGSDFVELYVGVGASRVRDLFKVAKQSAPCIIFIDEIDAVGRQRGAGMGGGNDEREQTLNQLLVEMDGFSANLGIIIMAATNRPDVLDPALLRPGRFDRQITMQVPDQKSREEILKVHARSKKLDPTIKFSEVAMRIPGFTGADIENLLNEAALLAARESRTVISMQDIDEAADRVTMGPAKKSRKYSPNEKKMVAYHEAGHAVIGLKVNLASTVQKVTIVPRGRAGGYALYTPVEEKFNYAKSELLAMITSALGGRVAEEIMFDDVTTGAYDDFKRATKLARSMVTEYGMSDLGPIQYESDSGNVFLGRDYLKDKNFSDAVALEIDREVRAIITECYEHARKVINENKNLLDNIAKYLIAVETLTKTDIDEIAATGQLQWWDNREVEEDSKKSE |
Enzyme Length | 641 |
Uniprot Accession Number | A9NE17 |
Absorption | |
Active Site | ACT_SITE 445; /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 222..229; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
Features | Active site (1); Chain (1); Metal binding (3); Nucleotide binding (1); 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 | 70,955 |
Kinetics | |
Metal Binding | METAL 444; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 448; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 520; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458 |
Rhea ID | |
Cross Reference Brenda |