NQRC_CHLMU
ID NQRC_CHLMU Reviewed; 318 AA.
AC Q9PKB5;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=TC_0551;
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_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; AE002160; AAF39390.1; -; Genomic_DNA.
DR PIR; C81690; C81690.
DR RefSeq; WP_010230817.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PKB5; -.
DR SMR; Q9PKB5; -.
DR STRING; 243161.TC_0551; -.
DR EnsemblBacteria; AAF39390; AAF39390; TC_0551.
DR GeneID; 1245911; -.
DR KEGG; cmu:TC_0551; -.
DR eggNOG; COG2869; Bacteria.
DR HOGENOM; CLU_870677_0_0_0; -.
DR OMA; GLWDAIY; -.
DR OrthoDB; 730368at2; -.
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: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; Sodium; Sodium transport; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..318
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT C"
FT /id="PRO_0000214212"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
FT MOD_RES 281
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
SQ SEQUENCE 318 AA; 34772 MW; C154D6BACEAFDF50 CRC64;
MASKSRHYLN QPWYIILFIF VLSLVAGTLL SSVSYVLSPI QKQAAEFDRN QQMLMAAQII
SYDNKFQIYA EGDWQPAVYN TKKQILEKSS STPPQVTVAT LCSYFQNFVR VLLTDSQGNL
SSFEDHNLNL EEFLSHPTSS VQDHSLHVIY AILANDESSK KLSSSQVAKN PVSIESIILP
IKGFGLWGPI YGFLALEKDG NTVLGTCWYQ HGETPGLGAN ITNPQWQQNF RGKKVFLASS
SGETDFAKTT LGLEVIKGSV SALLGDSPKA NSAVDGISGA TLTCNGVTEA FANSLAPYRP
LLTFFANLNS SGESHDNQ
