RSXD_SALTI
ID RSXD_SALTI Reviewed; 352 AA.
AC Q8Z6Q8;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 119.
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};
GN OrderedLocusNames=STY1666, t1324;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD01911.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68974.1; -; Genomic_DNA.
DR RefSeq; NP_456074.1; NC_003198.1.
DR RefSeq; WP_000231887.1; NZ_WSUR01000011.1.
DR AlphaFoldDB; Q8Z6Q8; -.
DR SMR; Q8Z6Q8; -.
DR STRING; 220341.16502753; -.
DR EnsemblBacteria; AAO68974; AAO68974; t1324.
DR KEGG; stt:t1324; -.
DR KEGG; sty:STY1666; -.
DR PATRIC; fig|220341.7.peg.1676; -.
DR eggNOG; COG4658; Bacteria.
DR HOGENOM; CLU_042020_0_0_6; -.
DR OMA; GWQWINL; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000074461"
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 69..91
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 215..235
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; 38234 MW; 3FBED7F3412628E7 CRC64;
MVFRIASSPY THNQRQTSRI MLLVLIAALP GIAAQTWFFG WGTLFQIVLA AITALVAEAI
VLRLRKQSVA SHLQDYSALL TGLLLAVSIP PLAPWWMVVL GTGFAIIIAK QLYGGLGQNP
FNPAMIGYVV LLISFPVQMT SWLPPYEIAA TTPDILDTLR MIFSGHTASG GDMTLLRIGI
DGISQATPLD TFKTSLRAGH SVEQIMQYPI YSGALAGVGW QWVNLAWLVG GVFLLWQKAI
RWHIPVSFLL TLALCAALGW LFSPATLASP QLHLLSGATM LGAFFILTDP VTASTTNRGR
LIFGALAGVL VWLIRSFGGY PDGVAFAVLL ANITVPLIDY YTRPRVYGHR KG
