(data stored in SCRATCH zone)

SWISSPROT: A4ATH5_MARSH

ID   A4ATH5_MARSH            Unreviewed;       249 AA.
AC   A4ATH5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   16-JAN-2019, entry version 64.
DE   RecName: Full=Na(+)-translocating NADH-quinone reductase subunit C {ECO:0000256|HAMAP-Rule:MF_00427};
DE            Short=Na(+)-NQR subunit C {ECO:0000256|HAMAP-Rule:MF_00427};
DE            Short=Na(+)-translocating NQR subunit C {ECO:0000256|HAMAP-Rule:MF_00427};
DE            EC=7.2.1.1 {ECO:0000256|HAMAP-Rule:MF_00427};
DE   AltName: Full=NQR complex subunit C {ECO:0000256|HAMAP-Rule:MF_00427};
DE   AltName: Full=NQR-1 subunit C {ECO:0000256|HAMAP-Rule:MF_00427};
GN   Name=nqrC {ECO:0000256|HAMAP-Rule:MF_00427};
GN   OrderedLocusNames=FB2170_16711 {ECO:0000313|EMBL:EAR00745.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00745.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00745.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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:0000256|HAMAP-Rule:MF_00427}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol +
CC         n Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-
CC         COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.2.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00427};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00427};
CC   -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE
CC       and NqrF. {ECO:0000256|HAMAP-Rule:MF_00427}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00427}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00427}.
CC   -!- SIMILARITY: Belongs to the NqrC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00427}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00427}.
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DR   EMBL; CP002157; EAR00745.1; -; Genomic_DNA.
DR   RefSeq; WP_013304548.1; NC_014472.1.
DR   STRING; 313603.FB2170_16711; -.
DR   EnsemblBacteria; EAR00745; EAR00745; FB2170_16711.
DR   KEGG; fbc:FB2170_16711; -.
DR   eggNOG; ENOG4106I92; Bacteria.
DR   eggNOG; COG2869; LUCA.
DR   HOGENOM; HOG000273678; -.
DR   KO; K00348; -.
DR   OMA; GLWDAIW; -.
DR   OrthoDB; 730368at2; -.
DR   BioCyc; MSP313603:G1GNS-119-MONOMER; -.
DR   Proteomes; UP000001602; 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   SMART; SM00900; FMN_bind; 1.
DR   TIGRFAMs; TIGR01938; nqrC; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4ATH5.
DR   SWISS-2DPAGE; A4ATH5.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00427};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00427};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Sodium {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Sodium transport {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00427};
KW   Ubiquinone {ECO:0000256|HAMAP-Rule:MF_00427}.
FT   TRANSMEM     12     33       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00427}.
FT   DOMAIN      138    239       FMN_bind. {ECO:0000259|SMART:SM00900}.
FT   COILED       26     46       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     222    222       FMN phosphoryl threonine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00427}.
SQ   SEQUENCE   249 AA;  27357 MW;  66C1AEC3DD3B6A0F CRC64;
     MAINTDKNSY TVIFAAVMVV IVGTVLAFLA SSLSDKIKEN ERLEKQQNIL YAMGINENEG
     EGSVSFIPTD KVAGEFTKYI KAQLIIEGDK ITKDDQAYLI DLKKQATAAK NGETRKLPLF
     VGNKDGADFY IIPMRGKGLW DAIWGFVALD DDMVVQGVYF DHAAETPGLG ANIKQRYFMD
     DFTGESILSG TQYEGIAVAK GNNDPLNEIK DDNEVDALAG ATITGNGVSD MIRESVNLYK
     DYLETIRVK
//

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