Entry sw:NQRC_VIBCB

ID   NQRC_VIBCB              Reviewed;         261 AA.
AC   Q9RFV9; A7N1U4;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 4.
DT   02-NOV-2016, entry version 105.
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=1.6.5.8 {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};
GN   OrderedLocusNames=VIBHAR_03273;
OS   Vibrio campbellii (strain ATCC BAA-1116 / BB120).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=338187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11 AND
RP   213-222, AND MASS SPECTROMETRY.
RX   PubMed=10587447; DOI=10.1021/bi991664s;
RA   Zhou W., Bertsova Y.V., Feng B., Tsatsos P., Verkhovskaya M.L.,
RA   Gennis R.B., Bogachev A.V., Barquera B.;
RT   "Sequencing and preliminary characterization of the Na+-translocating
RT   NADH:ubiquinone oxidoreductase from Vibrio harveyi.";
RL   Biochemistry 38:16246-16252(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N.,
RA   Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C.,
RA   Irgon J., Wilson R.K.;
RL   Submitted (AUG-2007) 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
CC       of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE
CC       are probably involved in the second step, the conversion of
CC       ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00427}.
CC   -!- CATALYTIC ACTIVITY: NADH + ubiquinone + n Na(+)(In) = NAD(+) +
CC       ubiquinol + n Na(+)(Out). {ECO:0000255|HAMAP-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
CC       and 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   -!- MASS SPECTROMETRY: Mass=28120; Method=MALDI; Range=2-261;
CC       Evidence={ECO:0000269|PubMed:10587447};
CC   -!- SIMILARITY: Belongs to the NqrC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00427}.
DR   EMBL; AF165980; AAF15413.1; -; Genomic_DNA.
DR   EMBL; CP000789; ABU72221.1; -; Genomic_DNA.
DR   RefSeq; WP_012128721.1; NC_022269.1.
DR   STRING; 338187.VIBHAR_03273; -.
DR   EnsemblBacteria; ABU72221; ABU72221; VIBHAR_03273.
DR   GeneID; 5554442; -.
DR   KEGG; vca:M892_14730; -.
DR   KEGG; vha:VIBHAR_03273; -.
DR   PATRIC; 20133177; VBIVibHar24526_3118.
DR   eggNOG; ENOG4106I92; Bacteria.
DR   eggNOG; COG2869; LUCA.
DR   HOGENOM; HOG000273678; -.
DR   KO; K00348; -.
DR   OMA; IKGITYY; -.
DR   Proteomes; UP000008152; Chromosome I.
DR   GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
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-HAMAP.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00427; NqrC; 1.
DR   InterPro; IPR007329; FMN-bd.
DR   InterPro; IPR010204; NqrC.
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   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Flavoprotein; FMN; Ion transport; Membrane;
KW   NAD; Oxidoreductase; Phosphoprotein; Sodium; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:10587447}.
FT   CHAIN         2    261       Na(+)-translocating NADH-quinone
FT                                reductase subunit C.
FT                                /FTId=PRO_0000214224.
FT   TRANSMEM     12     32       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00427}.
FT   MOD_RES     229    229       FMN phosphoryl threonine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00427}.
FT   CONFLICT     16     16       V -> I (in Ref. 1; AAF15413).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       148    246       ismart:FMN_bind [T]
FT   MYHIT         6    258       ihamap:NqrC [T]
FT   MYHIT       148    243       ipfam:FMN_bind [T]
SQ   SEQUENCE   261 AA;  27791 MW;  CE8016D1422C4745 CRC64;
     MASNNDSIKK TLGVVVGLSL VCSIIVSTAA VGLRDQQKAN AVLDKQSKIV EVAGIDAEGK
     KVPELFAEYI EPRLVDFKTG DFVEKAEDGS TAANYDQRKA AKDPAESIKL TADEDKAKIL
     RRANTGIVYL VKNGDDISKV IIPVHGNGLW SMMYAFVAVE TDGNTVSGIT YYEQGETPGL
     GGEVENPVWR AQFVGKKLFD ENHKPAIKIV KGGAPEGSEH GVDGLSGATL TGNGVQGTFD
     FWLGDMGFGP FLAKVRDGGL N
//