ID A0A3T0MZZ9_9RHOB Unreviewed; 590 AA.
AC A0A3T0MZZ9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Na(+)/H(+) antiporter subunit D {ECO:0000313|EMBL:AZV77340.1};
GN ORFNames=EBB79_05180 {ECO:0000313|EMBL:AZV77340.1};
OS Parasedimentitalea marina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Parasedimentitalea.
OX NCBI_TaxID=2483033 {ECO:0000313|EMBL:AZV77340.1, ECO:0000313|Proteomes:UP000283063};
RN [1] {ECO:0000313|EMBL:AZV77340.1, ECO:0000313|Proteomes:UP000283063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W43 {ECO:0000313|EMBL:AZV77340.1,
RC ECO:0000313|Proteomes:UP000283063};
RA Cao J.;
RT "Parasedimentitalea marina sp. nov., a psychrophilic bacterium isolated
RT from deep seawater of the New Britain Trench.";
RL Submitted (OCT-2018) 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|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
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DR EMBL; CP033219; AZV77340.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T0MZZ9; -.
DR KEGG; sedi:EBB79_05180; -.
DR OrthoDB; 9811798at2; -.
DR Proteomes; UP000283063; Chromosome.
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 Gene3D; 1.20.5.2700; -; 1.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR42682; HYDROGENASE-4 COMPONENT F; 1.
DR PANTHER; PTHR42682:SF4; NADH-UBIQUINONE_PLASTOQUINONE; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..21
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 28..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 413..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..379
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 590 AA; 63653 MW; 683F4F668FCA9749 CRC64;
MIEGLHPALL MLLGALVLPL FRGIWQKVLS VLVPVLALIA VAQISPGSSA EFRFAGVDLV
MFQADQLSLV FAWVFAIMAV IGNIYAWHIN DTGQRVSAFL YIGSAFGVVF AGDWFTLLVA
WEVMAFASAY LIFASASKAA VAAGFRYLMV HVAGGVLLFG GIILHGVQTG SYLTGPLDHG
AGGLAYNLIL ISFMLNAAVP PLSAWLTDAY PEATVTGAVF LSAFTTKTAV YVLIRNYPGA
EVLVGFGVAM ALYGVVFAVL ENDCRRLLGY HIISQVGYMV AAVGMGTEMA LNGAASHAFA
HILYKGLLFM GAGAVILMTG RRKLTEMGGL YRTMPITVFL YMIGALAISA FPLFSGFVSK
SMIISAANGD HRAAVALLLT VASSGTFLHT GLKLPYYMFF GKDCGLRPAE PPVNMLLAMG
LAALFCIGIG VFPQLLYAQL PYPVDYHPYS GSHVTESLGL LMFTLLAFVL FLKYLDPEKT
ISLDTDWFYR RGASLFMWIA RRPVLIWEQW LITLGDGAGL RLMHRLSRVS LRLDTQVIDA
AVNGVALTAL RLGMLLRHLQ SGIVSHYALA MIVGLILLFG WPLYVAMGAP
//
