ID A0A0B4XTU8_9GAMM Unreviewed; 644 AA. AC A0A0B4XTU8; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 28-MAR-2018, entry version 14. 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}; RX PubMed=23209202; DOI=10.1128/JB.01845-12; RA Lai Q., Shao Z.; RT "Genome sequence of an alkane-degrading bacterium, Alcanivorax RT pacificus 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 CC metallopeptidase for both cytoplasmic and membrane proteins. Plays CC a role in the quality control of integral membrane proteins. CC {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01458}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01458}; CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01458}; Cytoplasmic side {ECO:0000256|HAMAP- CC 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 CC M41 family. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase CC family. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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 HAMAP; MF_01458; FtsH; 1. DR InterPro; IPR003593; AAA+_ATPase. 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; 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}; KW 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 Complete proteome {ECO:0000313|Proteomes:UP000006764}; 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}; KW 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 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT DOMAIN 189 328 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 197 204 ATP. {ECO:0000256|HAMAP-Rule:MF_01458}. FT ACT_SITE 420 420 {ECO:0000256|HAMAP-Rule:MF_01458}. FT METAL 419 419 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 423 423 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 497 497 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT 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 //