ID A0A2R8CR72_9GAMM Unreviewed; 658 AA. AC A0A2R8CR72; DT 20-JUN-2018, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 1. DT 08-NOV-2023, entry version 21. DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458}; DE EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458}; GN Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458, GN ECO:0000313|EMBL:SPJ35294.1}; GN ORFNames=KSP9073_03353 {ECO:0000313|EMBL:SPJ35294.1}; OS Kushneria phyllosphaerae. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Kushneria. OX NCBI_TaxID=2100822 {ECO:0000313|EMBL:SPJ35294.1, ECO:0000313|Proteomes:UP000244934}; RN [1] {ECO:0000313|EMBL:SPJ35294.1, ECO:0000313|Proteomes:UP000244934} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EAod3 {ECO:0000313|EMBL:SPJ35294.1, RC ECO:0000313|Proteomes:UP000244934}; RA Keele B.F.; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|HAMAP- CC Rule:MF_01458}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01458}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01458}; CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01458}; CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. CC {ECO:0000256|RuleBase:RU003651}. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41 CC family. {ECO:0000256|ARBA:ARBA00010044, ECO:0000256|HAMAP- CC Rule:MF_01458}. CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family. CC {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01458}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ONZI01000005; SPJ35294.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2R8CR72; -. DR EnsemblBacteria; SPJ35294; SPJ35294; KSP9073_03353. DR OrthoDB; 9809379at2; -. DR Proteomes; UP000244934; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd19501; RecA-like_FtsH; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.30.720.210; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.20.58.760; Peptidase M41; 1. DR HAMAP; MF_01458; FtsH; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR005936; FtsH. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011546; Pept_M41_FtsH_extracell. DR InterPro; IPR000642; Peptidase_M41. DR InterPro; IPR037219; Peptidase_M41-like. DR NCBIfam; TIGR01241; FtsH_fam; 1. DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1. DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF17862; AAA_lid_3; 1. DR Pfam; PF06480; FtsH_ext; 1. DR Pfam; PF01434; Peptidase_M41; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF140990; FtsH protease domain-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00674; AAA; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01458}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP- KW Rule:MF_01458}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01458}. FT TRANSMEM 101..123 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 189..328 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT REGION 595..658 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 629..649 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 420 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 197..204 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 419 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 423 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 497 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" SQ SEQUENCE 658 AA; 72059 MW; E0CBFC87EE390485 CRC64; MNDMAKNLIL WLIIAAVLLT VFNNFSVDNS PQAMNYSQFV EQVQNKQIRQ VTIDGYDIRG ERDDGSSFQT IRPSAEDPRL MDDLLSNNVT VVGKKPDQQS IWSRLLIASF PILLILGIFL FFMRQMQGGG AGKGGPMSFG KSKAKLLSHE QVKTTFKDVA GCDEAKEEVE ELVDFLKDPS KFQRLGGQIP RGVLLVGPPG TGKTLLAKAI AGEARVPFFT ISGSDFVEMF VGVGASRVRD MFEQAKKQAP CIIFIDEIDA VGRSRGSGMG GGHDEREQTL NQLLVEMDGF EANEGIIIIA ATNRPDVLDP ALLRPGRFDR QVTVGLPDIR GREHILGVHL RKVPLADDVK PEMIARGTPG FSGAELANVV NEAALFAARK NRRLIGMAEL EMAKDKIMMG AEKRSMVMSE KEKRNTAYHE AGHAIIGLLM PEHDSVYKVT IIPRGRALGV TMFLPTEDRY SYTRQQIISQ ICSLFGGRIA EEMTLGPNGV TTGASNDIKR ATELAHNMVA KWGLSQEMGP LMYDEDESHQ FLGGPGGGGS KFTSAETSSR MDREIRRIID ECYQQAEQIL HDNRDKLDAM TDALIKFETI DADQINDIME GRDPRPPKEP GSSGPSGGLG VPDTSPSDVR PVEDPEDGDS ADDTRRRPSD PLGGSSGH //