RSXD_ECOLI
ID RSXD_ECOLI Reviewed; 352 AA.
AC P76182; Q2MB69;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305};
DE AltName: Full=Rsx electron transport complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305};
GN Name=rsxD {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000303|PubMed:12773378};
GN Synonyms=rnfD, ydgO; OrderedLocusNames=b1630, JW1622;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION, SUBUNIT, AND GENE NAME.
RX PubMed=12773378; DOI=10.1093/emboj/cdg252;
RA Koo M.S., Lee J.H., Rah S.Y., Yeo W.S., Lee J.W., Lee K.L., Koh Y.S.,
RA Kang S.O., Roe J.H.;
RT "A reducing system of the superoxide sensor SoxR in Escherichia coli.";
RL EMBO J. 22:2614-2622(2003).
CC -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC transfer with translocation of ions across the membrane (By
CC similarity). Required to maintain the reduced state of SoxR. Probably
CC transfers electron from NAD(P)H to SoxR (PubMed:12773378).
CC {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000269|PubMed:12773378}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00462};
CC -!- SUBUNIT: The complex is composed of six subunits: RsxA, RsxB, RsxC,
CC RsxD, RsxE and RsxG. {ECO:0000255|HAMAP-Rule:MF_00462,
CC ECO:0000305|PubMed:12773378}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00462}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00462}.
CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|HAMAP-
CC Rule:MF_00462}.
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DR EMBL; U00096; AAC74702.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76487.1; -; Genomic_DNA.
DR PIR; H64919; H64919.
DR RefSeq; NP_416147.1; NC_000913.3.
DR RefSeq; WP_000231927.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P76182; -.
DR SMR; P76182; -.
DR BioGRID; 4261729; 72.
DR STRING; 511145.b1630; -.
DR TCDB; 3.D.6.1.4; the ion (h(+) or na(+))-translocating nadh:ferredoxin oxidoreductase (nfo or rnf) family.
DR jPOST; P76182; -.
DR PaxDb; P76182; -.
DR EnsemblBacteria; AAC74702; AAC74702; b1630.
DR EnsemblBacteria; BAE76487; BAE76487; BAE76487.
DR GeneID; 946134; -.
DR KEGG; ecj:JW1622; -.
DR KEGG; eco:b1630; -.
DR PATRIC; fig|1411691.4.peg.631; -.
DR EchoBASE; EB3695; -.
DR eggNOG; COG4658; Bacteria.
DR HOGENOM; CLU_042020_0_0_6; -.
DR InParanoid; P76182; -.
DR OMA; GWQWINL; -.
DR PhylomeDB; P76182; -.
DR BioCyc; EcoCyc:G6874-MON; -.
DR PRO; PR:P76182; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-UniRule.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR HAMAP; MF_00462; RsxD_RnfD; 1.
DR InterPro; IPR004338; NqrB/RnfD.
DR InterPro; IPR011303; RnfD.
DR PANTHER; PTHR30578; PTHR30578; 1.
DR PANTHER; PTHR30578:SF0; PTHR30578:SF0; 1.
DR Pfam; PF03116; NQR2_RnfD_RnfE; 1.
DR TIGRFAMs; TIGR01946; rnfD; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Electron transport; Flavoprotein; FMN;
KW Membrane; Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..352
FT /note="Ion-translocating oxidoreductase complex subunit D"
FT /id="PRO_0000074453"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 78..109
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT MOD_RES 187
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
SQ SEQUENCE 352 AA; 38140 MW; 02F0EAFF8A5B4E70 CRC64;
MVFRIASSPY THNQRQTSRI MLLVLLAAVP GIAAQLWFFG WGTLVQILLA SVSALLAEAL
VLKLRKQSVA ATLKDNSALL TGLLLAVSIP PLAPWWMVVL GTVFAVIIAK QLYGGLGQNP
FNPAMIGYVV LLISFPVQMT SWLPPHEIAV NIPGFIDAIQ VIFSGHTASG GDMNTLRLGI
DGISQATPLD TFKTSVRAGH SVEQIMQYPI YSGILAGAGW QWVNLAWLAG GVWLLWQKAI
RWHIPLSFLV TLALCAMLGW LFSPETLAAP QIHLLSGATM LGAFFILTDP VTASTTNRGR
LIFGALAGLL VWLIRSFGGY PDGVAFAVLL ANITVPLIDY YTRPRVYGHR KG
