ID A0A365PS58_9PSED Unreviewed; 636 AA. AC A0A365PS58; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 11-DEC-2019, entry version 9. 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=hflB {ECO:0000313|EMBL:RBA55668.1}; GN Synonyms=ftsH {ECO:0000256|HAMAP-Rule:MF_01458, GN ECO:0000313|EMBL:RBA55668.1}; GN ORFNames=DQ403_15305 {ECO:0000313|EMBL:RBA55668.1}; OS Pseudomonas zhaodongensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1176257 {ECO:0000313|EMBL:RBA55668.1, ECO:0000313|Proteomes:UP000252554}; RN [1] {ECO:0000313|EMBL:RBA55668.1, ECO:0000313|Proteomes:UP000252554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SST2 {ECO:0000313|EMBL:RBA55668.1, RC ECO:0000313|Proteomes:UP000252554}; RA Abdel-Mageed W.M., Lehri B., Jarmusch S.A., Miranda K., Goodfellow M., RA Jaspars M., Karlyshev A.V.; RT "Whole genome sequencing of four bacterial strains from South Shetland RT trench revealing bio-synthetic gene clusters."; RL Submitted (JUN-2018) 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|HAMAP-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:RBA55668.1}. 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; QNTV01000012; RBA55668.1; -; Genomic_DNA. DR Proteomes; UP000252554; 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: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: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}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; 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 ECO:0000313|EMBL:RBA55668.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01458, ECO:0000313|EMBL:RBA55668.1}; 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 98..120 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 186..325 FT /note="AAA" FT /evidence="ECO:0000259|SMART:SM00382" FT NP_BIND 194..201 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT REGION 599..636 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 417 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 416 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 420 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 494 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" SQ SEQUENCE 636 AA; 69311 MW; 52FE5B7C68C92868 CRC64; MAKNLILWLI IAAVLVTVMN NFSSPTEPQT LNYSDFIEQV KEGQVERVTV DGFVITGKRS DGETFKTIRP AIQDNGLIGD LINNDVVIEG KQPEQQSIWT QLLVASFPIL VIIAVFMFFM RQMQGGAGGK GGPMSFGKSK ARLLSEDQVK TTFADVAGCD EAKEEVTELV EFLRDPGKFQ RLGGRIPRGV LMVGSPGTGK TLLAKAVAGE AKVPFFTISG SDFVEMFVGV GASRVRDMFE QAKKHAPCII FIDEIDAVGR HRGAGLGGGH DEREQTLNQL LVEMDGFEMN DGIIVIAATN RPDVLDPALL RPGRFDRQVV VGLPDIRGRE QILKVHMRKV PLGDTVEPAL IARGTPGFSG ADLANLVNEA SLFAARAGKR VVEMKEFELA KDKIMMGAER KSMVMSEKER LNTAYHEAGH AIVGRVVPEH DPVYKVSIIP RGRALGVTMF LPEEDRYSLS KRALISQICS LFGGRIAEEM TLGFEGVTTG ASNDIMRATQ LARNMVTKWG LSEKLGPLMY AEEEGEVFLG RSAGSQHTNV SGDTAKLIDL EVRSIIDQCY GTAKQILADN RDKLDVMAET LMKYETIDAD QIDDIMAGRT PREPRDWQDG SGPTGTPVQP EGGRPQTPIG GPAGEH //