ID A0A1G9GLA2_9RHOB Unreviewed; 512 AA.
AC A0A1G9GLA2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Multicomponent K+:H+ antiporter subunit D {ECO:0000313|EMBL:SDL01444.1};
GN ORFNames=SAMN05216257_1085 {ECO:0000313|EMBL:SDL01444.1};
OS Meinhardsimonia xiamenensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Meinhardsimonia.
OX NCBI_TaxID=990712 {ECO:0000313|EMBL:SDL01444.1, ECO:0000313|Proteomes:UP000199328};
RN [1] {ECO:0000313|Proteomes:UP000199328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10789 {ECO:0000313|Proteomes:UP000199328};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNFV01000008; SDL01444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9GLA2; -.
DR STRING; 990712.SAMN05216257_1085; -.
DR OrthoDB; 9768329at2; -.
DR Proteomes; UP000199328; 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:UP000199328};
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..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..265
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..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 128..424
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 512 AA; 53098 MW; 5BF59DEB736422CE CRC64;
MNHWIIVPVV LPALLAPLIA FVMRHDIVLA RSFSTAGTAA LAAVAVGLTL MAAGGQTHVY
ELGNWPAPFG IVLVLDRLSA MMVLLTAVLG MIVLAYAIGT GWDRRGQHFH ALFQFQLMGI
CGAFVTGDIF NLFVFFEVLL IASYGLMIHG GGKDRLRAGL QYVIMNLAGS TLFLFALGTI
YATTGTLNIA DLAQRVQEIP AEDSALVRVA AVLLMVVFAV KAALFPVQFW LPGTYSNAPA
PVAALFAIMT KVGAYAVLRV YAIVFPPETA ATGALPAGTL MVMALVTLAV GALGVLGARR
LLPLVSFSVL GSMGTLFIAL AGFAPETTVA ALFYLVHSTF AAAALFLVAD LVVSQRGEAA
DRLVTAPPAA QNGLLAALFF AGAIAMTGMP PLSGFLGKLL ILDAVRPSDH AVLLWTAILL
TSLLTIVGFA RAGSVIFWKS TELVGTGAGA GGEARPRAPG LALAAIGAIM AAFLTLTVLA
GPATAYLEQA AAQLHDPADY IEAVLSRAAG GS
//
