ID A0A1Q2CWU5_9ACTN Unreviewed; 516 AA.
AC A0A1Q2CWU5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Na+/H+ antiporter subunit D {ECO:0000313|EMBL:AQP50593.1};
GN ORFNames=BW733_06850 {ECO:0000313|EMBL:AQP50593.1};
OS Tessaracoccus flavescens.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=399497 {ECO:0000313|EMBL:AQP50593.1, ECO:0000313|Proteomes:UP000188235};
RN [1] {ECO:0000313|EMBL:AQP50593.1, ECO:0000313|Proteomes:UP000188235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SST-39T {ECO:0000313|EMBL:AQP50593.1,
RC ECO:0000313|Proteomes:UP000188235};
RX PubMed=18398170; DOI=10.1099/ijs.0.64868-0;
RA Lee D.W., Lee S.D.;
RT "Tessaracoccus flavescens sp. nov., isolated from marine sediment.";
RL Int. J. Syst. Evol. Microbiol. 58:785-789(2008).
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; CP019607; AQP50593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2CWU5; -.
DR STRING; 399497.BW733_06850; -.
DR KEGG; tfa:BW733_06850; -.
DR OrthoDB; 9768329at2; -.
DR Proteomes; UP000188235; 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:UP000188235};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 130..418
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 516 AA; 54398 MW; 2EB443338674479F CRC64;
MINLLPVPVL LAIFGAATTL VVPRRPGVQR LISVACLSGI VIVAGLFMYA TSTTGPMALW
LGGWAAPLGI ALVVDRLSAL MLLVASTVAL AVLIFATGQD KDEVRRETPV SIFHPTFLLL
VAGVSNAFLA GDLFNLFVGF EILLFASYVL LTLGGTADRV RAGTTYVIVS LLSSSLFLIS
ISAIYAATGT VNMAHLSVRL RDLTEPVQLL LEVLLLVTFA IKAAVFPLSS WLPDSYPTAP
APVTAVFAGL LTKVGVYAII RTETILFPLH TLDTVLLVAS GLTMVIGILG ALAQVEIKRM
LSFTLISHIG YMVFGIALNS TEALAATIFY TAHHITIQAT LFLVTGLIER RGGTSSLEGL
GGLLKTAPLL AFLFFVPAMN LGGIPPLSGF IGKLGLLQAG AGVGGPLVWT VMVAGVLTSL
LTLMAMAKVW NRAFWGVTPS EQRRQEAIAA NQDPEDVDGD DPRVMPPLQV GATVGLILFG
IALTVFAGPL YEYAHAAAET LRDGTVVSIV LPEGLR
//
