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NQRC_PSEAE
ID   NQRC_PSEAE              Reviewed;         261 AA.
AC   Q9HZK8;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Na(+)-translocating NADH-quinone reductase subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
DE            Short=Na(+)-NQR subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
DE            Short=Na(+)-translocating NQR subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
DE            EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00427};
DE   AltName: Full=NQR complex subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
DE   AltName: Full=NQR-1 subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
GN   Name=nqrC {ECO:0000255|HAMAP-Rule:MF_00427}; OrderedLocusNames=PA2997;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(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_00427}.
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_00427};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00427};
CC   -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC       NqrF. {ECO:0000255|HAMAP-Rule:MF_00427}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00427}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00427}.
CC   -!- SIMILARITY: Belongs to the NqrC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00427}.
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DR   EMBL; AE004091; AAG06385.1; -; Genomic_DNA.
DR   PIR; F83272; F83272.
DR   RefSeq; NP_251687.1; NC_002516.2.
DR   RefSeq; WP_003105182.1; NZ_QZGE01000009.1.
DR   AlphaFoldDB; Q9HZK8; -.
DR   SMR; Q9HZK8; -.
DR   STRING; 287.DR97_4941; -.
DR   PaxDb; Q9HZK8; -.
DR   PRIDE; Q9HZK8; -.
DR   DNASU; 880204; -.
DR   EnsemblBacteria; AAG06385; AAG06385; PA2997.
DR   GeneID; 880204; -.
DR   KEGG; pae:PA2997; -.
DR   PATRIC; fig|208964.12.peg.3145; -.
DR   PseudoCAP; PA2997; -.
DR   HOGENOM; CLU_077882_0_1_6; -.
DR   InParanoid; Q9HZK8; -.
DR   OMA; GLWDAIW; -.
DR   PhylomeDB; Q9HZK8; -.
DR   BioCyc; PAER208964:G1FZ6-3049-MON; -.
DR   PHI-base; PHI:8943; -.
DR   Proteomes; UP000002438; 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:UniProtKB-UniRule.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00427; NqrC; 1.
DR   InterPro; IPR007329; FMN-bd.
DR   InterPro; IPR010204; NqrC.
DR   PANTHER; PTHR37838; PTHR37838; 1.
DR   Pfam; PF04205; FMN_bind; 1.
DR   PIRSF; PIRSF009437; NQR-1_subunit_C; 1.
DR   SMART; SM00900; FMN_bind; 1.
DR   TIGRFAMs; TIGR01938; nqrC; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Flavoprotein; FMN; Ion transport;
KW   Membrane; NAD; Phosphoprotein; Reference proteome; Sodium;
KW   Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..261
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   C"
FT                   /id="PRO_0000214220"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
FT   MOD_RES         230
FT                   /note="FMN phosphoryl threonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
SQ   SEQUENCE   261 AA;  27780 MW;  8B265BA05D7661C4 CRC64;
     MANQESTTRT LLVALVVCLV SSVFVAGAAV ALKPTQAENR LLDKQRSILA IAGLGEPGMS
     GKEVKALFDS RITAKVVDLQ SGTFSDAQDP LGYDPLKAAK DPALSDALPA AEDIASIKRR
     ERYTTVYLVE TDGKLDTLIL PVRGYGLWST LYGFLALKGD LNTVAGFGFY QHGETPGLGG
     EVDNPKWKAL WVGKTLYDAQ GDLAVQIIKG SVDPQSAKAT HQVDGLAGAT LTSKGVDNLL
     HFWLGKDGFD AFLANLRKGE A
 
 
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