ID   RSXD_ESCF3              Reviewed;         352 AA.
AC   B7LQP0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=EFER_1413;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ88933.1; -; Genomic_DNA.
DR   RefSeq; WP_000231900.1; NC_011740.1.
DR   AlphaFoldDB; B7LQP0; -.
DR   SMR; B7LQP0; -.
DR   EnsemblBacteria; CAQ88933; CAQ88933; EFER_1413.
DR   KEGG; efe:EFER_1413; -.
DR   HOGENOM; CLU_042020_0_0_6; -.
DR   OMA; GWQWINL; -.
DR   OrthoDB; 1654433at2; -.
DR   BioCyc; EFER585054:EFER_RS07150-MON; -.
DR   Proteomes; UP000000745; 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_1000125386"
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        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        89..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        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        244..264
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;  38039 MW;  C4BA56ADE4854F10 CRC64;
     MVFRIASSPY THNQRQTSRI MLLVLLAAIP GIATQLWFFG WGTLVQIILA VISALSAEAL
     VLKLRNQPIA AILKDNSALL TGLLLAVSIP PLAPWWMVVL GTVFAVIIAK QLYGGLGQNP
     FNPAMIGYVV LLISFPVQMT NWLPPYEIAA TVPGMADTLQ VIFTGHTTSG GDMSTLRMGI
     DGISQATPLD TLKTSLHSGR SVEQIMQYPI FSGMLAGAGW QWVNLAWLAG GVWLLAIKVI
     RWHIPVSFLV SLALCATLGW LFAPESLASP QIHMLSGATM LGAFFILTDP VTASTTNRGR
     LIFGALAGVL VWLIRSFGGY PDGVAFAVLL ANITVPLIDY YTRPRVYGHR KG