ID A0A238Y3P2_9RHOB Unreviewed; 547 AA.
AC A0A238Y3P2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Multisubunit potassium/proton antiporter, PhaD subunit {ECO:0000313|EMBL:SNR65592.1};
GN ORFNames=SAMN06265378_11453 {ECO:0000313|EMBL:SNR65592.1};
OS Paracoccus sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1214787 {ECO:0000313|EMBL:SNR65592.1, ECO:0000313|Proteomes:UP000198409};
RN [1] {ECO:0000313|Proteomes:UP000198409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26170 {ECO:0000313|Proteomes:UP000198409};
RA Varghese N., Submissions S.;
RL Submitted (JUN-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; FZNM01000014; SNR65592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238Y3P2; -.
DR OrthoDB; 9768329at2; -.
DR Proteomes; UP000198409; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
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 33..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..442
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 547 AA; 56970 MW; 4F1C33CFD02F663F CRC64;
MIGEHLIIAP ILIPFVTGAL MLLYDDRRRA AKFWLSIVSA AAQLLIAVQL VIRAKTGGDV
SDWEGISFYL LGDWAAPYGI VLVLDRLAAM MLVLTGLLAI PSLVYAHAGW NRQGPHYYSL
FQFLLMGLNG AFLTGDLFNL FVFFEILLAA SYGLLLHGSG QLRVRAGMHY IAINLAASLL
FLIGVSLIYG VTGTLNMAHL ANLIAAMPGE NRPLLHAAVA VLAVAFLVKA GSWPLSFWLP
TAYMAAAAPV GAMFAIMTKV GIYAIVRLSM LLFGDTGGAS AGFGAGILII LGMATVLFGL
LGVLSSQGLG RMAAHSVLIS SGTVLGITGF ALAGGGPGML AGALYYLVAS TLATSALFLL
IEPMSREDGG IAAMLALTAD AYGLDGADLD EVPDAGLAIP ATMTVLGICF ALCVLMLAGL
PPLPGFIGKI AMVQALMAQT ALPAGLAWSF IALLILSGFA TLIGMARIGI QTFWSGDLVL
PRVLALEIAP VIALLAVLAM TTVKAEAMLR YTAGTAQALH DTAAYAFGVF ATPRAADRAP
DDQGDDP
//
