ID A0A2M8P168_9CHLR Unreviewed; 633 AA. AC A0A2M8P168; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 02-DEC-2020, entry version 11. 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 Candidatus Thermofonsia Clade 1 bacterium. OC Bacteria; Chloroflexi; Candidatus Thermofonsia; OC Candidatus Thermofonsia Clade 1. OX NCBI_TaxID=2364210 {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 Horizontal RT Gene Transfer."; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. 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: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 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; IPR000642; Peptidase_M41. DR InterPro; IPR037219; Peptidase_M41-like. DR Pfam; PF00004; AAA; 1. DR Pfam; PF17862; AAA_lid_3; 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: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 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 95..116 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 179..318 FT /note="AAA" FT /evidence="ECO:0000259|SMART:SM00382" FT NP_BIND 187..194 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT REGION 592..633 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 554..581 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 596..623 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 410 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 409 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 413 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 489 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule: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 //