RSXD_SHIFL
ID RSXD_SHIFL Reviewed; 352 AA.
AC Q83KY5; Q7C1G6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=SF1655, S1787;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN43237.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17123.1; -; Genomic_DNA.
DR RefSeq; NP_707530.1; NC_004337.2.
DR RefSeq; WP_000231904.1; NZ_WPGW01000065.1.
DR AlphaFoldDB; Q83KY5; -.
DR SMR; Q83KY5; -.
DR STRING; 198214.SF1655; -.
DR EnsemblBacteria; AAN43237; AAN43237; SF1655.
DR EnsemblBacteria; AAP17123; AAP17123; S1787.
DR GeneID; 1024858; -.
DR KEGG; sfl:SF1655; -.
DR KEGG; sft:NCTC1_01793; -.
DR KEGG; sfx:S1787; -.
DR PATRIC; fig|198214.7.peg.1951; -.
DR HOGENOM; CLU_042020_0_0_6; -.
DR OMA; GWQWINL; -.
DR OrthoDB; 1654433at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..352
FT /note="Ion-translocating oxidoreductase complex subunit D"
FT /id="PRO_0000298240"
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..318
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; 38098 MW; E247ACA3B0EFBF3A CRC64;
MVFRIASSPY THNQRQTSRI MLLVLLAAVP GIAAQLRFFG WGTLVQILLA SVSALLAEAL
VLKLRKQSVA ATLKDNSALL TGLLLAVSIP PLAPWWMVVL GTVFAVIIAK QLYGGLGQNP
FNPAMIGYVV LLISFPVQMT SWLPPHEIAV NIPGFIDAIQ VIFSGHTASG GDMNTLRLGI
DGISQATPLD TFKTSVRAGH SVEQIMQYPI YSGILAGAGW QWVNLAWLAG GVWLLWQKAI
RWHIPLSFLV TLALCATLGW LFSPETLAAP QIHLLSGATM LGAFFILTDP VTASTTNRGR
LMFGALAGLL VWLIRSFGGY PDGVAFAVLL ANITVPLIDY YTRPRVYGHR KG
