Detail Information for IndEnz0002003107
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;