AC MF_01458; DC Protein; auto TR HAMAP; MF_01458; -; 1; level=0 XX Names: FtsH XX ID FTSH DE RecName: Full=ATP-dependent zinc metalloprotease FtsH; DE EC=3.4.24.-; GN Name=ftsH; XX case CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase. else CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for CC both cytoplasmic and membrane proteins. Plays a role in the quality CC control of integral membrane proteins. end case case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; end case CC -!- SUBUNIT: Homohexamer. case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi- CC pass membrane protein; Stromal side. else case and not CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane CC protein; Stromal side. else case (defined and ) or CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein; CC Cytoplasmic side. else case not defined or CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein; CC Cytoplasmic side. end case CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41 CC family. XX DR PROSITE; PS00674; AAA; 1; trigger=no DR Pfam; PF00004; AAA; 1; trigger=no DR Pfam; PF06480; FtsH_ext; 1; trigger=no DR Pfam; PF01434; Peptidase_M41; 1; trigger=no DR NCBIfam; TIGR01241; FtsH_fam; 1; trigger=no DR General; Transmembrane; -; 2; trigger=yes case and not DR ADD_TOPO_DOMAIN; Cytoplasmic; -; 2; trigger=yes DR ADD_TOPO_DOMAIN; Lumenal; -; 1; trigger=yes else case DR ADD_TOPO_DOMAIN; Stromal; -; 2; trigger=yes DR ADD_TOPO_DOMAIN; Lumenal; -; 1; trigger=yes else case (defined and ) or DR ADD_TOPO_DOMAIN; Cytoplasmic; -; 2; trigger=yes DR ADD_TOPO_DOMAIN; Periplasmic; -; 1; trigger=yes else case not defined or DR ADD_TOPO_DOMAIN; Cytoplasmic; -; 2; trigger=yes DR ADD_TOPO_DOMAIN; Extracellular; -; 1; trigger=yes end case XX KW ATP-binding case or and not KW Thylakoid else case (defined and ) or KW Cell inner membrane KW Cell membrane else case not defined or KW Cell membrane end case KW Hydrolase KW Membrane KW Metal-binding KW Metalloprotease KW Nucleotide-binding KW Protease KW Transmembrane KW Transmembrane helix KW Zinc XX GO GO:0005524; F:ATP binding GO GO:0016887; F:ATP hydrolysis activity GO GO:0008233; F:peptidase activity GO GO:0030163; P:protein catabolic process case GO GO:0008270; F:zinc ion binding end case case GO GO:0009535; C:chloroplast thylakoid membrane else case and not GO GO:0042651; C:thylakoid membrane else GO GO:0005886; C:plasma membrane end case XX FT From: FTSH_AQUAE (O67077) FT BINDING 195..202 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-x-[PT]-G-[TVS]-G-K-T FT ACT_SITE 419 FT Condition: E FT BINDING 418 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 422 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 496 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: D XX Size: 510-854; Related: None; Template: P0AAI3; O67077; Q9WZ49; Q5SI82; Q55700; Scope: Bacteria Plastid Fusion: Nter: Cter: None Duplicate: in ALKMQ, BDEBA, CONWI, MERI4, PETMO, PHYMT, RHOBA, SALRM, SORC5, SPHTD, SYMTH, THEPX, THERP, SYNY3 Plasmid: in ACAM1, PARP8, THERP Comments: Chlamydiota have an N-terminal extension not found in other organisms. Not all proteins have 2 transmembrane domains. There are short paralogs in Haemophilus that are missing the N-terminal transmembrane section, they are annotated as atypical. Some plastids encode very long homologs that cannot bind zinc, they are annotated as atypical (CHLVU, HELSJ, OLTVI). XX # Revision 1.14 2023/06/01 //