ID A0A1F8DTV2_9BACT Unreviewed; 613 AA. AC A0A1F8DTV2; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 15-MAR-2017, entry version 2. 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=A2935_01775 {ECO:0000313|EMBL:OGM92053.1}; OS Candidatus Wolfebacteria bacterium RIFCSPLOWO2_01_FULL_47_17b. OC Bacteria; Candidatus Wolfebacteria. OX NCBI_TaxID=1802558 {ECO:0000313|EMBL:OGM92053.1, ECO:0000313|Proteomes:UP000177011}; RN [1] {ECO:0000313|EMBL:OGM92053.1, ECO:0000313|Proteomes:UP000177011} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27774985; DOI=10.1038/ncomms13219; RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J., RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., RA Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected RT biogeochemical processes in an aquifer system."; RL Nat. Commun. 7:13219-13219(2016). 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OGM92053.1}. 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; MGIS01000024; OGM92053.1; -; Genomic_DNA. DR Proteomes; UP000177011; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. 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 Pfam; PF00004; AAA; 1. DR Pfam; PF06480; FtsH_ext; 1. DR Pfam; PF01434; Peptidase_M41; 1. DR SMART; SM00382; AAA; 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:OGM92053.1}; KW Cell division {ECO:0000313|EMBL:OGM92053.1}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Complete proteome {ECO:0000313|Proteomes:UP000177011}; 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 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 110 133 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT DOMAIN 196 335 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 204 211 ATP. {ECO:0000256|HAMAP-Rule:MF_01458}. FT ACT_SITE 427 427 {ECO:0000256|HAMAP-Rule:MF_01458}. FT METAL 426 426 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 430 430 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 502 502 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. SQ SEQUENCE 613 AA; 67616 MW; ADC42DEF08259FB7 CRC64; MKSSKIIKNL FVTILVFISV ILLFSSVYTA GEQPQIISLS ELAQKIQADE VRSLTVEENT VTATLSDDSI TETHKEAETS LTETLGQFGV SSEQLSQIAI TVQEPSGWKF WSGILLPTLI PILVIGFLFW FMFRQARSGA SQALSFGKSN IRLFAPFKDR ITFADVAGAT EAKQELVEVV DFLKNSKKYL DLGAQIPRGV LLLGPPGTGK TLLARAVAGE AQVPYFHISA SEFVEMFVGV GASRTRDAFQ TAKKAAPSIL FIDEIDAIGR ERGAGLGGGH DEREQTLNQI LVEMDGFDKE AQVVVLAATN RPDILDPALL RPGRFDRRVI LDLPDLKDRE AILKIHGRNK KLAKDIDYTR IAQRTPGFSG ADLANLMNEG AILAARKNKK VVAQDDLYEA VEKVILGPER RSRVFGKKEK EITAYHEAGH ALVAASLKDA DPVHKVSIIA RGQAGGYTLK LPIEDRYLKT RKQFLADLAV TFGGYATEEI MFKDISTGAS NDLSVASEIT RKMVSKYGMS EKFGPITFGK TQELIFLGRE ISNEKNYSES VAAEIDKEVS SIIEKAYNAA KKIITKRKSA LEAIAKELMK KETLERDDFD ALIKQFKFKL IEV //