ID A0A222E1G6_9RHOB Unreviewed; 531 AA.
AC A0A222E1G6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Na(+)/H(+) antiporter subunit D {ECO:0000313|EMBL:ASP19808.1};
GN Name=mrpD {ECO:0000313|EMBL:ASP19808.1};
GN ORFNames=ANTHELSMS3_01093 {ECO:0000313|EMBL:ASP19808.1};
OS Antarctobacter heliothermus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Antarctobacter.
OX NCBI_TaxID=74033 {ECO:0000313|EMBL:ASP19808.1, ECO:0000313|Proteomes:UP000203589};
RN [1] {ECO:0000313|EMBL:ASP19808.1, ECO:0000313|Proteomes:UP000203589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS3 {ECO:0000313|EMBL:ASP19808.1,
RC ECO:0000313|Proteomes:UP000203589};
RA Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA Clarke A.K.;
RT "Genome Sequence of Antarctobacter heliothermus Strain SMS3 Isolated from a
RT culture of the Diatom Skeletonema marinoi.";
RL Submitted (JUL-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; CP022540; ASP19808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222E1G6; -.
DR KEGG; aht:ANTHELSMS3_01093; -.
DR OrthoDB; 9768329at2; -.
DR Proteomes; UP000203589; 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 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:UP000203589};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 128..405
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 531 AA; 56249 MW; DF4666B184E7DFE0 CRC64;
MNHWIIAPVV LPALLAPLLG YVMRHDIVLA RVASAAGTVA LFFIALGLAF WAADGGTHVY
RLGNWPAPFG IVLVLDRLSA MMVLLTATLA LIVLWHAIAT GWDAKGRHFH ALYQFQLMGI
CGAFLTGDAF NLFVFFEVLL IASYGLMVHS GGKVRLQAGL QYLVMNLAGS TLFLFALGTM
YATTGTLNMA DLAVKVPLMP ADEGAMVRVA AVLLLIVFMI KAALFPVQFW LPGTYANAPA
PVAALFAIMT KVGAYAIIRL HTLAYGPQSS PTAGLVEEWL FPAALVTVAL GAIGVLAAKR
LMPLLSFSVI GSMGTLMLAV APQSPYATET ALYYLVHSTL SAAALFLLAD LVISRRGTDT
LSVRPPVLQN GLFAALFFGG AIAMAGMPPL SGFLGKLLIL DALRDPHLMP WAWSGILLGS
LVTLVGFARA GSMLFWKSTA VIVPEGAEPI DAEPRPAPAT TAEVAPTVAL LALLAALAVL
AGPATNYMRA AGNQLFEPEG YIDAVLAPVE KPEELDSLKI DKPDPLAEEE H
//
