ID A0A365PS58_9PSED Unreviewed; 636 AA. AC A0A365PS58; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 31-JUL-2019, entry version 8. 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 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: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 Complete proteome {ECO:0000313|Proteomes:UP000252554}; 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, KW 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 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT DOMAIN 186 325 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 194 201 ATP. {ECO:0000256|HAMAP-Rule:MF_01458}. FT REGION 599 636 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT ACT_SITE 417 417 {ECO:0000256|HAMAP-Rule:MF_01458}. FT METAL 416 416 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 420 420 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 494 494 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT 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 //