Detail Information for IndEnz0002018676
IED ID IndEnz0002018676
Enzyme Type ID protease018676
Protein Name ATP-dependent zinc metalloprotease FtsH
EC 3.4.24.-
Gene Name ftsH hflB bbp_345
Organism Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Erwiniaceae Buchnera (aphid P-endosymbionts) Buchnera aphidicola Buchnera aphidicola (Baizongia pistaciae) Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Enzyme Sequence MAKNLMLWLVIAVVLMSIFQNFSANNINNRKIDYSTFLSDVNQDQVREVHISGREMNIIRKDNGRYITYIPISDPKLLDNLLVKNVKIIGAAPEEQSFFTAIFISWFPMLLLIGVWVFFMRQMQVGGGKGAMSFGKSKARMLPEDQVKITFSDVAGCDEAKEEVQELVEYLKEPSRFQKLGGKIPKGILMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEHSRKVAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFDGNEGIILIAATNRPDVLDPALLRPGRFDRQIFVALPDIRGREKIIQVHMKKVPLGNNVDPMIIARGTPGFSGADLANLVNEAALFAARNNRDVVMMSDFESAKDKITMGSERRSMVMTEKQKESTAYHEAGHVIVGRLVPEHDPAHKVTIIPRGRALGVTFFLPKDDVLSINKNKLESQISTLYGGRLAEEIIYGVNNVSTGAHNDIKVATNLARNMVTQWGFSKKLGPLLYSEEEGEIFLGRTVTKSKHMSDETARIIDEEVKLLVEKNYNRAKKILEENLDILHAMKDALIKYETINSRQIDDLMKRKSIQSSNICTDDDNN
Enzyme Length 610
Uniprot Accession Number Q89AF2
Absorption
Active Site ACT_SITE 415; /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 192..199; /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 68,020
Kinetics
Metal Binding METAL 414; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 418; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 492; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458
Rhea ID
Cross Reference Brenda