ID A0A0B4XTU8_9GAMM Unreviewed; 644 AA. AC A0A0B4XTU8; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 11-DEC-2019, entry version 20. 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 ORFNames=S7S_16525 {ECO:0000313|EMBL:AJD49717.1}; OS Alcanivorax pacificus W11-5. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD49717.1, ECO:0000313|Proteomes:UP000006764}; RN [1] {ECO:0000313|EMBL:AJD49717.1, ECO:0000313|Proteomes:UP000006764} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W11-5 {ECO:0000313|EMBL:AJD49717.1, RC ECO:0000313|Proteomes:UP000006764}; RX PubMed=23209202; DOI=10.1128/JB.01845-12; RA Lai Q., Shao Z.; RT "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus RT type strain W11-5, isolated from deep sea sediment."; RL J. Bacteriol. 194:6936-6936(2012). 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|HAMAP-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; CP004387; AJD49717.1; -; Genomic_DNA. DR MEROPS; M41.001; -. DR EnsemblBacteria; AJD49717; AJD49717; S7S_16525. DR KEGG; apac:S7S_16525; -. DR KO; K03798; -. DR Proteomes; UP000006764; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:ATPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 1.20.58.760; -; 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 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; SSF140990; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01241; FtsH_fam; 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}; Cell cycle {ECO:0000313|EMBL:AJD49717.1}; KW Cell division {ECO:0000313|EMBL:AJD49717.1}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Hydrolase {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|HAMAP-Rule:MF_01458}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; Protease {ECO:0000256|HAMAP-Rule:MF_01458}; KW Reference proteome {ECO:0000313|Proteomes:UP000006764}; 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..122 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 189..328 FT /note="AAA" FT /evidence="ECO:0000259|SMART:SM00382" FT NP_BIND 197..204 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT REGION 602..644 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 420 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 419 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 423 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 497 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" SQ SEQUENCE 644 AA; 70524 MW; A92D68570C7A095F CRC64; MNDMTKNIVL WLVIAGVLYV VAQGISHEPT VQTVDYSEFI KRVENGGVAR VEIQDYRIRG EDRQGKLFET VKPPVADLDL MPTLIQNNVR VEGKEPERQG FMTQLFLSVL PILLILAIFI FFMRQMQGGG KGGGGPMTFG KSKARLLSED QIKTTFADVA GVEEAKEEVQ ELVEFLRDPA KFQRLGGRIP RGVLMVGSPG TGKTLLAKAI AGEARVPFFS ISGSDFVEMF VGVGASRVRD MFEQAKKHAP CIIFIDEIDA VGRSRGAGLG GGHDEREQTL NQLLVEMDGF GANDGIIVIA ATNRPDVLDA ALLRPGRFDR QVVVPLPDVR GREQIIKVHM RNVPVADDVN PSLIARGTPG FSGADLANLV NEAALFAARG NKRLVSMEEF ERAKDKILMG AERRSMVMNE KEKLNTAYHE AGHAIIGRVV PEHDPVYKVS IIPRGRALGV TMYLPTEDKY SQSKRALESM ICSLFGGRIA EEMINGFDGV TTGASNDIER ATKLARAMVT KWGLSEKLGP LAYEEEEGEV FLGKTMSQTK HVSEEIAQEI DREVRAIIDD CYGRAKQILE DNRDKLETMA QALMQYETID ADQIEDIMNG RQVRPPKDWQ DPGPGTGSPS TGAAPDGEPT PKGEGPIGGP ANTH //