ID   RNFD_BUCAT              Reviewed;         347 AA.
AC   B8D721;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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};
GN   OrderedLocusNames=BUAPTUC7_115;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=561501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuc7;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
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}.
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DR   EMBL; CP001158; ACL29936.1; -; Genomic_DNA.
DR   RefSeq; WP_010895954.1; NC_011834.1.
DR   AlphaFoldDB; B8D721; -.
DR   SMR; B8D721; -.
DR   KEGG; bau:BUAPTUC7_115; -.
DR   HOGENOM; CLU_042020_0_0_6; -.
DR   OMA; GWQWINL; -.
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..347
FT                   /note="Ion-translocating oxidoreductase complex subunit D"
FT                   /id="PRO_1000191668"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        114..134
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        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT   MOD_RES         182
FT                   /note="FMN phosphoryl threonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
SQ   SEQUENCE   347 AA;  39559 MW;  1C6F68F2A002F9F2 CRC64;
     MNFPCIYHVY SIRKIMFLVI VACLPGIFAK YYFFGIGTLI QIFFSIFISL VLEIIILKIR
     SKNIKNYLQD TSLVLTSVLF GVSIPPLLPW WMTSIGLFFA IVVAKHLYGG IGQNIFNPAM
     VGYAVLLISF PVYMNNWNER DFSLSFFNDF KKSAYIIFFK NDITTVSSSY LNIIPDAFTT
     ATPLNNFKIK SHLKDDFFLK ENIIKNKEVS IQTSWKCINI SFFLGGIFLL FTKIICWRIP
     ISFLSSLGML SIITYFYSKE LFMSPQVHFF SGGTMICAFF IATDPVTAAC NNVGKIVFGI
     IIGFLVWIIR NYSDYPDAIA FSVLFANMTV PLVDYYTKSS GYGRNNI