NQRB_CHLMU
ID NQRB_CHLMU Reviewed; 503 AA.
AC Q9PKB6;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit B {ECO:0000255|HAMAP-Rule:MF_00426};
DE Short=Na(+)-NQR subunit B {ECO:0000255|HAMAP-Rule:MF_00426};
DE Short=Na(+)-translocating NQR subunit B {ECO:0000255|HAMAP-Rule:MF_00426};
DE EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00426};
DE AltName: Full=NQR complex subunit B {ECO:0000255|HAMAP-Rule:MF_00426};
DE AltName: Full=NQR-1 subunit B {ECO:0000255|HAMAP-Rule:MF_00426};
GN Name=nqrB {ECO:0000255|HAMAP-Rule:MF_00426}; OrderedLocusNames=TC_0550;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00426};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00426};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00426}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00426}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00426}.
CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|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; AE002160; AAF39389.1; -; Genomic_DNA.
DR PIR; B81690; B81690.
DR RefSeq; WP_010230815.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PKB6; -.
DR SMR; Q9PKB6; -.
DR STRING; 243161.TC_0550; -.
DR EnsemblBacteria; AAF39389; AAF39389; TC_0550.
DR GeneID; 1245910; -.
DR KEGG; cmu:TC_0550; -.
DR eggNOG; COG1805; Bacteria.
DR HOGENOM; CLU_042020_1_1_0; -.
DR OMA; FNPAYPE; -.
DR OrthoDB; 1654433at2; -.
DR Proteomes; UP000000800; Chromosome.
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: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; PTHR30578; 1.
DR Pfam; PF03116; NQR2_RnfD_RnfE; 1.
DR TIGRFAMs; TIGR01937; nqrB; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Flavoprotein; FMN; Ion transport;
KW Membrane; NAD; Phosphoprotein; Sodium; Sodium transport; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..503
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT B"
FT /id="PRO_0000074433"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT MOD_RES 248
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
SQ SEQUENCE 503 AA; 54969 MW; 6C9293E3842028AA CRC64;
MLEKFVDSLW KFCRKSKFQY MTPVADAVDS FCFEPLHTPS SPPFVRDAVD VKRWMMLVVI
ALMPTVFVAI WNSGLQALVY QSSDPQIMEA FLHISGFTSY FSFVSKEIGI ASVLFAGCKI
FLPLLFISYA VGGTCEVLFA IIRKHKIAEG LLVTGMLYPL ILPPTIPYWM AALGIAFGVV
IGKELFGGTG MNILNPALTG RAFLFFTFPA KMSGDVWVGS NPSKIKESLA MMNSLAERSN
FDGFSQSTCL QILNSTPPSV KRVHIDAIAS NILKLEHVPS QEVLQSQFST WAESFPGLTV
DQLSLDQLQN FVTSPTAEGG LGLLPAHFDA AYSLTDAIYG IGKFSTGNLF FGNIVGSLGE
TSTVACLLGA GLLLLTGIAS WRTMLSFGLS SLFFAWLFKI ISILAAGQSG AWAPAKFFIP
VYRHLFIGGL AFGLVFMATD PVTSPATKLA KWFYGAFIGF LTILIRLINP AYPEGVMLAI
LLGNVFAPSF DRIALKQYRQ RRV
