ID   RNFD_YERE8              Reviewed;         351 AA.
AC   A1JM66;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Rnf electron transport complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462};
GN   Name=rnfD {ECO:0000255|HAMAP-Rule:MF_00462}; OrderedLocusNames=YE1990;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane.
CC       {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: RnfA, RnfB, RnfC,
CC       RnfD, RnfE and RnfG. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM286415; CAL12069.1; -; Genomic_DNA.
DR   RefSeq; YP_001006243.1; NC_008800.1.
DR   AlphaFoldDB; A1JM66; -.
DR   SMR; A1JM66; -.
DR   STRING; 393305.YE1990; -.
DR   EnsemblBacteria; CAL12069; CAL12069; YE1990.
DR   KEGG; yen:YE1990; -.
DR   PATRIC; fig|393305.7.peg.2152; -.
DR   eggNOG; COG4658; Bacteria.
DR   HOGENOM; CLU_042020_0_0_6; -.
DR   OMA; GWQWINL; -.
DR   BioCyc; YENT393305:G13HL-1936-MON; -.
DR   Proteomes; UP000000642; 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..351
FT                   /note="Ion-translocating oxidoreductase complex subunit D"
FT                   /id="PRO_0000298243"
FT   TRANSMEM        18..38
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        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   MOD_RES         185
FT                   /note="FMN phosphoryl threonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
SQ   SEQUENCE   351 AA;  38074 MW;  A5CC998028C0F027 CRC64;
     MQIASSPFTH NQRSTRSIML LVILACIPGI IAQTYFFGYG SLIQVALAIM TAVLAEGAVL
     HLRKQPVLTR LQDNSALLTG LLLGISLPPL APWWMIVLGT AFAIIIAKQL YGGLGQNPFN
     PAMVGYVVLL ISFPVQMTSW LPPLPLQGTP VGFYDSLLTI FTGFTQNGAD IHQLQIGYDG
     ISQATPLDNF KTSLRSQPVE QILQQPIFTA GLAGIGWQWI NLGFLAGGLL LLWRKAIHWH
     IPVSFLLALA GCAAISWMIA PHSFAPPMLH LFSGATMLGA FFIATDPVSA STTPRGRLIF
     GALIGILVWL IRVYGGYPDG VAFAVLLANI CVPLIDHYTQ PRVYGHQRGH K