ID A0A1F8DTV2_9BACT Unreviewed; 613 AA. AC A0A1F8DTV2; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 02-DEC-2020, entry version 13. 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., Brodie E.L., RA Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected biogeochemical RT processes in an aquifer system."; RL Nat. Commun. 7:13219-13219(2016). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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: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: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: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:OGM92053.1}; KW Cell division {ECO:0000313|EMBL:OGM92053.1}; 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 110..133 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 196..335 FT /note="AAA" FT /evidence="ECO:0000259|SMART:SM00382" FT NP_BIND 204..211 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT ACT_SITE 427 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 426 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 430 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 502 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule: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 //