RSXD_ECO57
ID RSXD_ECO57 Reviewed; 352 AA.
AC P58325;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=Z2639, ECs2339;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG56619.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35762.1; -; Genomic_DNA.
DR PIR; C90921; C90921.
DR PIR; G85769; G85769.
DR RefSeq; NP_310366.1; NC_002695.1.
DR RefSeq; WP_000231928.1; NZ_SWKA01000004.1.
DR AlphaFoldDB; P58325; -.
DR SMR; P58325; -.
DR STRING; 155864.EDL933_2585; -.
DR EnsemblBacteria; AAG56619; AAG56619; Z2639.
DR EnsemblBacteria; BAB35762; BAB35762; ECs_2339.
DR GeneID; 913023; -.
DR KEGG; ece:Z2639; -.
DR KEGG; ecs:ECs_2339; -.
DR PATRIC; fig|386585.9.peg.2448; -.
DR eggNOG; COG4658; Bacteria.
DR HOGENOM; CLU_042020_0_0_6; -.
DR OMA; GWQWINL; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000074454"
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; 38110 MW; D6D6A89BAC0F7E68 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 TLALCATLGW LFSPETLAAP QIHLLSGATM LGAFFILTDP VTASTTNRGR
LIFGALAGLL VWLIRSFGGY PDGVAFAVLL ANITVPLIDY YTRPRVYGHR KG
