Detail Information for IndEnz0002018657
IED ID IndEnz0002018657
Enzyme Type ID protease018657
Protein Name ATP-dependent zinc metalloprotease FtsH
EC 3.4.24.-
Gene Name ftsH Amuc_0348
Organism Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc)
Taxonomic Lineage cellular organisms Bacteria PVC group Verrucomicrobia Verrucomicrobiae Verrucomicrobiales Akkermansiaceae Akkermansia Akkermansia muciniphila Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc)
Enzyme Sequence MPPSPPRPPKFPGSGRPESPNWGVWVMVLLIVGVLAFGFFTPESFGLGPRKENLESFEAQYKAGRVVLNDPKAPVEVVLSENGSEGVIHALVYRKEIQPKVEMTPFALTYSMSLPDRDKPLLNELSGYRVVESPYRTEEGKNVSLIPEGAQKLSVPEFNRLALEGRIAGGKDGIILAEDGNQNVLVGQIVTRIWPAATGDASVDKQRFERVEVPFTLEFQGDRVKQLLGPDTKFKRESGSWGGILLNLLPIVLILVILFFMFRAQSGGARGAMSFGKSRARLISPDKNKVTFKDVAGISEAKEEVWELVEFLRNPEKFRDLGATIPRGVLMVGAPGTGKTLLARAIAGESNASFYSISGSDFVEMFVGVGASRVRDMFEQAKRTAPSLIFIDEIDAVGRQRGYGMGGGNDEREQTLNALLVEMDGFENNSNVIVIAATNRADILDPALLRPGRFDRQVVVNLPDVRGREQILQVHARKVKMAPGVSFERIARGTSGFSGAQLANLVNEAALLAARKGLKEITEAELEEARDKVSWGRERRSLAINERGRRITAVHEAGHAICLLKTPHSEPLHRVTIVPRGGALGMTMWLPSDDKMHQLRSEMLDQLVVAMGGRCAEQIVFGDVTSGATGDIKSATNLARRMVCEFGMSEKLGLIEYGEHQGEVYIARDLGTRSRNYSESTAELIDSEVRFLVDSAYERAMAILTENRDKLDILTEALMEFETLEGSQVMDILEYGEMKNPPARVTPPPMPSEVEEQPGKDDSGHNEKKEAEETRADGAEERKMEEELEQAERAPFSYNPVDEFGKDGGEKK
Enzyme Length 812
Uniprot Accession Number B2UMY1
Absorption
Active Site ACT_SITE 556; /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 333..340; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_01458
Features Active site (1); Chain (1); Compositional bias (1); Metal binding (3); Nucleotide binding (1); Region (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 89,455
Kinetics
Metal Binding METAL 555; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 559; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458; METAL 631; /note=Zinc; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_01458
Rhea ID
Cross Reference Brenda