ID A0A2M8P168_9CHLR Unreviewed; 633 AA. AC A0A2M8P168; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 23-MAY-2018, 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=CUN51_04735 {ECO:0000313|EMBL:PJF31297.1}; OS Chloroflexi bacterium. OC Bacteria; Chloroflexi. OX NCBI_TaxID=2026724 {ECO:0000313|EMBL:PJF31297.1, ECO:0000313|Proteomes:UP000228921}; RN [1] {ECO:0000313|EMBL:PJF31297.1, ECO:0000313|Proteomes:UP000228921} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CP2_2F {ECO:0000313|EMBL:PJF31297.1}; RA Ward L.M., Hemp J., Shih P.M., Mcglynn S.E., Fischer W.; RT "Evolution of Phototrophy in the Chloroflexi Phylum Driven by RT Horizontal Gene Transfer."; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. 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:PJF31297.1}. 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; PGTK01000004; PJF31297.1; -; Genomic_DNA. DR Proteomes; UP000228921; Unassembled WGS sequence. 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; IPR000642; Peptidase_M41. DR InterPro; IPR037219; Peptidase_M41-like. DR Pfam; PF00004; AAA; 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:PJF31297.1}; KW Cell division {ECO:0000313|EMBL:PJF31297.1}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000228921}; 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 95 116 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT DOMAIN 179 318 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 187 194 ATP. {ECO:0000256|HAMAP-Rule:MF_01458}. FT COILED 554 581 {ECO:0000256|SAM:Coils}. FT ACT_SITE 410 410 {ECO:0000256|HAMAP-Rule:MF_01458}. FT METAL 409 409 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 413 413 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 489 489 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. SQ SEQUENCE 633 AA; 69082 MW; B7CD27E724A351CD CRC64; MAIFLGVRGG GSSGSELKLS ELAQQIISGT PRISAIAVAQ NEVRVTYAGS SRPPAITRKD PSMPLPEQLI SLGVPKELVA QLPIEYVQPN DITPFFSILV SLLPIILIAG FFFLMLRQAQ GSNNQAISFG KSRARMFTGD RPTVTFDDVA GADEAKEELR EVVEFLKEPD KFVQLGARIP KGVLLIGSPG TGKTLLAKAV AGEAGVPFFS ISGSEFVEMF VGVGASRVRD LFDQAKRHSP CIIFIDEIDA VGRHRGAGLG GSHDEREQTL NQILVEMDGF DTDTNVIVIA ATNRPDILDP ALMRPGRFDR RVVLDRPDVK GREAILRVHS RGKPLAADVD LAVLSRTTPG FVGADLENLM NEAAILAARK NKKTISMRDC EEAIYRVVLG PERKSRVISE EQKRLVAYHE AGHAIVGHFL PNCDPIRKIT IVPRGISGGS VLSVPEDDMG PETRARIEDA IAQALGGRAA EAIVFGEVTT GAGGGNGSDL ATVTRYARAM VTRFGMSDRL GPMIFGQKEE MVFLGREIAE QRDYSEAIAE IIDEEVKKIV DEAYQRALAV LTEHREELER VAQRLMEVET IDYEEFMQLM GESPATNRRK RPEMLPKPAE KPATQREQRD DLPPRMGTAA SPA //