ID A0A1Y5T5I6_9RHOB Unreviewed; 513 AA.
AC A0A1Y5T5I6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Na(+)/H(+) antiporter subunit D {ECO:0000313|EMBL:SLN54545.1};
GN Name=mrpD {ECO:0000313|EMBL:SLN54545.1};
GN ORFNames=PEL8287_02916 {ECO:0000313|EMBL:SLN54545.1};
OS Roseovarius litorisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN54545.1, ECO:0000313|Proteomes:UP000193827};
RN [1] {ECO:0000313|EMBL:SLN54545.1, ECO:0000313|Proteomes:UP000193827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN54545.1,
RC ECO:0000313|Proteomes:UP000193827};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000256|ARBA:ARBA00002378}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000320}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU000320}.
CC -!- SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit D
CC family. {ECO:0000256|ARBA:ARBA00005346}.
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DR EMBL; FWFL01000007; SLN54545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5T5I6; -.
DR OrthoDB; 9768329at2; -.
DR Proteomes; UP000193827; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR42703:SF1; NA(+)_H(+) ANTIPORTER SUBUNIT D1; 1.
DR PANTHER; PTHR42703; NADH DEHYDROGENASE; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000193827};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 127..421
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 513 AA; 54329 MW; 9F51F4ACB9457EB8 CRC64;
MTHWIILPVV LPAILAPFIV LAARYHIGIQ RVFSIVGVGA LIAIAAGLAW QASDGTVTVY
RLSDWAAPFG IVLVGDRLST MMVLLTAVLA LLVLLYAIGS GWDDRGRHFH ALFQFQLMGI
MGAFLTGDLF NLFVFFEVLL IASYGLMIHA GGNARLRAGV QYVLFNLLGS TLFLFALGSI
YAETGTLNMA DLAQRVALID PAASVGIRVA SVLLLLVFAI KAAVVPLHFW LPSSYAEAPA
PVAALFAIMT KVGAYAIIRV YTLIFPPDLE VTVGLHGMWL LPAALISLAI GMVGVLAARK
LDRLVAFAVI GSMGMVMVAI SIFTPTSVAA ALYYIIHSTF AAAALFLIVD LVRSGRDNLE
LKAVAPISGA ALTAALYFTA AIAMTGLPPL SGFVGKLLIL DASFSSPLVV WTWAIILSAS
LISIVGFARA GSTVFWKAES IAHPVEATLP MRPAALSYVA VGGLLGLLIA HTIFAGPVHA
YMNAMSEQLF APEPYISTVL DTPGKLSTPK EAH
//
