ID A0A7G9L728_9FLAO Unreviewed; 400 AA. AC A0A7G9L728; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 22-FEB-2023, entry version 7. DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit B {ECO:0000256|HAMAP-Rule:MF_00426}; DE Short=Na(+)-NQR subunit B {ECO:0000256|HAMAP-Rule:MF_00426}; DE Short=Na(+)-translocating NQR subunit B {ECO:0000256|HAMAP-Rule:MF_00426}; DE EC=7.2.1.1 {ECO:0000256|HAMAP-Rule:MF_00426}; DE AltName: Full=NQR complex subunit B {ECO:0000256|HAMAP-Rule:MF_00426}; DE AltName: Full=NQR-1 subunit B {ECO:0000256|HAMAP-Rule:MF_00426}; GN Name=nqrB {ECO:0000256|HAMAP-Rule:MF_00426}; GN ORFNames=H9W90_09450 {ECO:0000313|EMBL:QNM84427.1}; OS Polaribacter pectinis. OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae. OX NCBI_TaxID=2738844 {ECO:0000313|EMBL:QNM84427.1, ECO:0000313|Proteomes:UP000515808}; RN [1] {ECO:0000313|EMBL:QNM84427.1, ECO:0000313|Proteomes:UP000515808} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L12M9 {ECO:0000313|EMBL:QNM84427.1, RC ECO:0000313|Proteomes:UP000515808}; RA Jeong Y.S.; RT "Polaribacter sp. L12M9 isolated from gut of the Korean scallop."; RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to CC ubiquinol by two successive reactions, coupled with the transport of CC Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are CC probably involved in the second step, the conversion of ubisemiquinone CC to ubiquinol. {ECO:0000256|HAMAP-Rule:MF_00426}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n CC Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565, CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, CC ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=7.2.1.1; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00426}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00426, CC ECO:0000256|PIRSR:PIRSR016055-50}; CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and CC NqrF. {ECO:0000256|HAMAP-Rule:MF_00426}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00426}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00426}. CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000256|HAMAP- CC Rule:MF_00426}. 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; CP060695; QNM84427.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7G9L728; -. DR KEGG; ppec:H9W90_09450; -. DR Proteomes; UP000515808; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR HAMAP; MF_00426; NqrB; 1. DR InterPro; IPR010966; NqrB. DR InterPro; IPR004338; NqrB/RnfD. DR PANTHER; PTHR30578; ELECTRON TRANSPORT COMPLEX PROTEIN RNFD; 1. DR PANTHER; PTHR30578:SF1; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT B; 1. DR Pfam; PF03116; NQR2_RnfD_RnfE; 1. DR PIRSF; PIRSF016055; NADH-UbQ_OxRdtase_B_su; 1. DR TIGRFAMs; TIGR01937; nqrB; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00426}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP- KW Rule:MF_00426}; KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_00426}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW Rule:MF_00426}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00426}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00426}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP- KW Rule:MF_00426}; Sodium {ECO:0000256|HAMAP-Rule:MF_00426}; KW Sodium transport {ECO:0000256|HAMAP-Rule:MF_00426}; KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP- KW Rule:MF_00426}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00426}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00426}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00426}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_00426, ECO:0000313|EMBL:QNM84427.1}. FT TRANSMEM 56..77 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00426" FT TRANSMEM 98..124 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00426" FT TRANSMEM 144..165 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00426" FT TRANSMEM 242..265 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00426" FT TRANSMEM 272..290 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00426" FT TRANSMEM 310..328 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00426" FT TRANSMEM 340..358 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00426" FT TRANSMEM 364..384 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00426" FT MOD_RES 220 FT /note="FMN phosphoryl threonine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00426, FT ECO:0000256|PIRSR:PIRSR016055-50" SQ SEQUENCE 400 AA; 44037 MW; 7A28D5AE9B45EFF2 CRC64; MGLKQNLHNL KEKYKGTKMA PAFNAIHTFL YLPNEVTHKG GTHIKAADDL KRTMNIVIMA LIPCLIFGMF NAGYQHYAAI DGSLRTDVLA NFFTFDNLWI GIIKVLPLVI VSYGVGLLVE FIFAVIKGHE VEEGYLVTGM LVPLIVPVDT PLWMLAVAVV FGVVIGKEVF GGTGMNILNP ALTIRAFLFF AYPTWMSGDK VWVYDAVERT GTADAISGET ILGSYAQNQE VIYSTWDKFA GFIPGSIGET STLLILLGAA FLIFTKIGSW RIIVSTFIGA AVMGLIFNQI VAADIITESS KFYGLMNTVW WEHLMIGGLA FGAVFMATDP VTASQTNKGK WIYGFLIGFI SIMIRVFNPA YPEGVFLAIL LMNVFAPTID HYVVQGNVKK RLKRTKVKTA //