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Database: UniProt
Entry: A0A3N6MP48_9BURK
LinkDB: A0A3N6MP48_9BURK
Original site: A0A3N6MP48_9BURK 
ID   A0A3N6MP48_9BURK        Unreviewed;       552 AA.
AC   A0A3N6MP48;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Monovalent cation/H+ antiporter subunit D {ECO:0000313|EMBL:RQH05489.1};
GN   ORFNames=D1Y85_15680 {ECO:0000313|EMBL:RQH05489.1};
OS   Paraburkholderia dinghuensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2305225 {ECO:0000313|EMBL:RQH05489.1, ECO:0000313|Proteomes:UP000272778};
RN   [1] {ECO:0000313|EMBL:RQH05489.1, ECO:0000313|Proteomes:UP000272778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DHOA04 {ECO:0000313|EMBL:RQH05489.1,
RC   ECO:0000313|Proteomes:UP000272778};
RA   Gao Z.-H., Qiu L.-H., Fu J.-C.;
RT   "Paraburkholderia sp. DHOA04, isolated from soil.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RQH05489.1}.
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DR   EMBL; RQIS01000010; RQH05489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N6MP48; -.
DR   OrthoDB; 9768329at2; -.
DR   Proteomes; UP000272778; 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:UP000272778};
KW   Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        31..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        161..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..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..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        417..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        450..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          125..350
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   552 AA;  57165 MW;  AE4EA92D1CE96A29 CRC64;
     MNHALVLPIV IPLVAAAAIV ALPLRAQRLQ RALSVIATLA LVPVAVWLAR LASSGDVVTY
     ALGAWPAPFG IVLQLDRLAA LMLLLTAVLA GCCLLGTSSA DVRRGRYFRA LFQFELMGLN
     GAFLAGDLFN LFVFFELLLI ASYALLLHGG GRRRVMSGLR YMLLNLVGSS FFLIAVGVLY
     GLTGTLNMAD MGVRLAHLDA ASLPLAQFAG AMLMLVFGVK AAVFPLSFWL PQAYRSAIGP
     VAALFAIMTK VGVYAMLRCD ALVFGAAGGI LEGFMHNWAW WLAIATIVFG ALGALAVSSL
     KTTTAYLVLV SVGLLIAAAS LQNATAWSAL LYYLISTTLC SAALFLLADT LEPEAPDPAA
     AASEPTSHAA LDDTTAPAIS SEPDGETAVA EVAVTAVTAV VQAVSPARTA TPWPSKAAAL
     LYLALAVGAA GLPPLSGFLG KAMVLAATPV AQAVVLWPAV LISGLLLIVA LSRTGTRIFW
     AVPAAQAFSD EAPPTAPRGT PAKLAACALL LACVLAVTLS AGPLKHYLDA TAAQLLDRAA
     YVRAVLNAPE NG
//
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