RNFD_VIBC3
ID RNFD_VIBC3 Reviewed; 348 AA.
AC A5F2R1; C3LZ25;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Ion-translocating oxidoreductase complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305};
DE AltName: Full=Rnf electron transport complex subunit D {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305};
GN Name=rnfD {ECO:0000255|HAMAP-Rule:MF_00462};
GN OrderedLocusNames=VC0395_A0535, VC395_1029;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
RN [3]
RP COFACTOR, PROSTHETIC GROUP AT THR-187, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP MUTAGENESIS OF THR-187 AND THR-278.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=18831535; DOI=10.1021/bi800920j;
RA Backiel J., Juarez O., Zagorevski D.V., Wang Z., Nilges M.J., Barquera B.;
RT "Covalent binding of flavins to RnfG and RnfD in the Rnf complex from
RT Vibrio cholerae.";
RL Biochemistry 47:11273-11284(2008).
RN [4]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=25831459; DOI=10.1021/acs.biochem.5b00020;
RA Hreha T.N., Mezic K.G., Herce H.D., Duffy E.B., Bourges A., Pryshchep S.,
RA Juarez O., Barquera B.;
RT "Complete topology of the RNF complex from Vibrio cholerae.";
RL Biochemistry 54:2443-2455(2015).
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:0000250|UniProtKB:A5F5X0,
CC ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000305|PubMed:18831535};
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, ECO:0000269|PubMed:18831535,
CC ECO:0000269|PubMed:25831459}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00462, ECO:0000269|PubMed:18831535,
CC ECO:0000269|PubMed:25831459}.
CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|HAMAP-
CC Rule:MF_00462}.
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DR EMBL; CP000627; ABQ21410.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP09041.1; -; Genomic_DNA.
DR RefSeq; WP_000863737.1; NZ_JAACZH010000005.1.
DR AlphaFoldDB; A5F2R1; -.
DR SMR; A5F2R1; -.
DR STRING; 345073.VC395_1029; -.
DR EnsemblBacteria; ABQ21410; ABQ21410; VC0395_A0535.
DR KEGG; vco:VC0395_A0535; -.
DR KEGG; vcr:VC395_1029; -.
DR PATRIC; fig|345073.21.peg.999; -.
DR eggNOG; COG4658; Bacteria.
DR HOGENOM; CLU_042020_0_0_6; -.
DR OMA; GWQWINL; -.
DR Proteomes; UP000000249; Chromosome 2.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Electron transport; Flavoprotein; FMN;
KW Membrane; Phosphoprotein; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..348
FT /note="Ion-translocating oxidoreductase complex subunit D"
FT /id="PRO_1000081161"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18831535,
FT ECO:0000305|PubMed:25831459"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TOPO_DOM 65..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18831535,
FT ECO:0000305|PubMed:25831459"
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TOPO_DOM 92..94
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:18831535,
FT ECO:0000269|PubMed:25831459"
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TOPO_DOM 118..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18831535,
FT ECO:0000305|PubMed:25831459"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TOPO_DOM 147..213
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:18831535,
FT ECO:0000305|PubMed:25831459"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TOPO_DOM 235..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18831535,
FT ECO:0000305|PubMed:25831459"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TOPO_DOM 264..265
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:25831459,
FT ECO:0000305|PubMed:18831535"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TOPO_DOM 287..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18831535,
FT ECO:0000305|PubMed:25831459"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462"
FT TOPO_DOM 342..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18831535,
FT ECO:0000269|PubMed:25831459"
FT MOD_RES 187
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00462,
FT ECO:0000305|PubMed:18831535"
FT MUTAGEN 187
FT /note="T->V: Abolishes flavin binding."
FT /evidence="ECO:0000269|PubMed:18831535"
FT MUTAGEN 278
FT /note="T->L: Can still bind flavin."
FT /evidence="ECO:0000269|PubMed:18831535"
SQ SEQUENCE 348 AA; 37604 MW; 5185136462A6466C CRC64;
MAFFIASSPH LRSKRSTADV MRWVLVCALP GLIAQTYFFG YGTLIQLLLA ISVAVALEAG
IMLLRKRSPI SALRDYSAVV TAWLLAVAIP PLSPWWVVVI GLIFAIVIAK HLYGGLGQNP
FNPAMIAYVV LLISFPVQMT SWMAPIKLTA EPSSLVDSFS LIFGGFDSDG LSLQQIRTGI
DGITMATPLD AIKTSLKAGH TMSETLTQPQ FSGFAGIGWE WVNIAYLLGG LILLKLRIIR
WHIPVAMLAG LVFTALLAQL FAPGTTASPM IHLLSGATML GAFFIATDPV SASTTDKGRL
IYGFFIGAMV FLIRSWGGFP DGVAFAVLLA NMCVPLIDYY TKPRTYGH
