ID A0A061SSA0_9RHOB Unreviewed; 515 AA.
AC A0A061SSA0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cation:proton antiporter {ECO:0000313|EMBL:KAJ02264.1};
GN ORFNames=PM02_14970 {ECO:0000313|EMBL:KAJ02264.1};
OS Sulfitobacter mediterraneus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=83219 {ECO:0000313|EMBL:KAJ02264.1, ECO:0000313|Proteomes:UP000027337};
RN [1] {ECO:0000313|EMBL:KAJ02264.1, ECO:0000313|Proteomes:UP000027337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1FIGIMAR09 {ECO:0000313|EMBL:KAJ02264.1,
RC ECO:0000313|Proteomes:UP000027337};
RX PubMed=24855294;
RA Mas-Llado M., Pina-Villalonga J.M., Brunet-Galmes I., Nogales B., Bosch R.;
RT "Draft Genome Sequences of Two Isolates of the Roseobacter Group,
RT Sulfitobacter sp. Strains 3SOLIMAR09 and 1FIGIMAR09, from Harbors of
RT Mallorca Island (Mediterranean Sea).";
RL Genome Announc. 2:e00350-14(2014).
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}.
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:KAJ02264.1}.
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DR EMBL; JEMU01000013; KAJ02264.1; -; Genomic_DNA.
DR RefSeq; WP_037909918.1; NZ_JEMU01000013.1.
DR AlphaFoldDB; A0A061SSA0; -.
DR STRING; 83219.PM02_14970; -.
DR eggNOG; COG0651; Bacteria.
DR Proteomes; UP000027337; 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:UP000027337};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..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..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 127..422
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 515 AA; 54496 MW; 5578CFA282AD1A8C CRC64;
MTHWIIAPVV LPALLAPFIV LAARYHIGIQ RVFSVAGVLS LIAIAAGLAW QASDGTIILY
QLSDWAAPFG IVLVGDRLST LMILLTAVLA LFVILYAIGS GWDKRGWHFH ALFQFQLMGI
MGAFLTGDVF NLFVFFEVLL IASYGLMIHG GGNLRLRAGV QYVLFNLLGS TLFLFALGAI
YAETGTLNMA DLAQRVALID PAESVGIRIA SVMLLLVFAI KAAVVPLHFW LPSSYAEAPA
PVAALFAIMT KVGAYAIIRV YTMVFAPDLD VTAGLHGLWL LPAALVSLAL GMIGVLAARK
LDRLVAFAVI GSMGMVMISI SLFSQAGIAA ALYYIVHSTL AAAALFLICD LVRAGRAHLN
LTAAPPVSGA ALTAALFFVA AIAMTGLPPL SGFVGKLMIL DAAFDTPLAI WTWAIILSAS
LISVVGFARA GSVLFWKASA ETLPEHEGQL PSPRPSVLSY AAVGGLLSLL ILHTVFAGPA
YRYADATAKQ LFDPAPYINK VLGTPGKLST PKEGH
//
