ID   RSXD_ECOL6              Reviewed;         352 AA.
AC   Q8FH94;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462};
DE            EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00462};
DE   AltName: Full=Rsx electron transport complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462};
GN   Name=rsxD {ECO:0000255|HAMAP-Rule:MF_00462}; OrderedLocusNames=c2022;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane. Required to
CC       maintain the reduced state of SoxR. {ECO:0000255|HAMAP-Rule:MF_00462}.
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   -!- 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; AE014075; AAN80482.1; -; Genomic_DNA.
DR   RefSeq; WP_000231933.1; NC_004431.1.
DR   AlphaFoldDB; Q8FH94; -.
DR   SMR; Q8FH94; -.
DR   STRING; 199310.c2022; -.
DR   EnsemblBacteria; AAN80482; AAN80482; c2022.
DR   KEGG; ecc:c2022; -.
DR   eggNOG; COG4658; Bacteria.
DR   HOGENOM; CLU_042020_0_0_6; -.
DR   OMA; GWQWINL; -.
DR   BioCyc; ECOL199310:C2022-MON; -.
DR   Proteomes; UP000001410; 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: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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Electron transport; Flavoprotein; FMN;
KW   Membrane; Phosphoprotein; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..352
FT                   /note="Ion-translocating oxidoreductase complex subunit D"
FT                   /id="PRO_0000298230"
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;  38156 MW;  2518BD9BBE8473F2 CRC64;
     MVFRIASSPY THNQRQTSRI MLLVLLAAVP GIAAQLWFFG WGTLVQILLA SVSALLAEAL
     VLKLRKQSVA ATLKDNSALL TGLLLAVSIP PLAPWWMVVL GTVFAVIIAK QLYGGLGQNP
     FNPAMIGYVV LLISFPVQMT SWLPPHEIAV NIPGFIDAIQ VIFSGHTASG GDMNTLRLGI
     DGISQATPLD TFKTSVRAGH SVEQIMQYPI YSGILAGVGW QWVNLAWLAG GVWLLWQKAI
     RWHIPLSFLV TLALCATLGW LFSPETLAAP QIHLLSGATM LGAFFILTDP VTASTTNRGR
     LIFGALAGLL VWMIRSFGGY PDGVAFAVLL ANITVPLIDY YTRPRVYGHR KG