ID Q6FF35_ACIAD Unreviewed; 602 AA.
AC Q6FF35;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE SubName: Full=pH adaptation potassium efflux system D transmembrane protein {ECO:0000313|EMBL:CAG67322.1};
GN Name=phaD {ECO:0000313|EMBL:CAG67322.1};
GN OrderedLocusNames=ACIAD0374 {ECO:0000313|EMBL:CAG67322.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG67322.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG67322.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67322.1; -; Genomic_DNA.
DR RefSeq; WP_004920446.1; NC_005966.1.
DR AlphaFoldDB; Q6FF35; -.
DR STRING; 202950.GCA_001485005_00637; -.
DR GeneID; 45232878; -.
DR KEGG; aci:ACIAD0374; -.
DR eggNOG; COG0651; Bacteria.
DR HOGENOM; CLU_007100_9_2_6; -.
DR OrthoDB; 9768329at2; -.
DR BioCyc; ASP62977:ACIAD_RS01750-MONOMER; -.
DR Proteomes; UP000000430; 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:UP000000430};
KW Transmembrane {ECO:0000256|RuleBase:RU000320, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 143..438
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT REGION 582..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 66749 MW; 90D2E60B579A23E9 CRC64;
MSDFITFWHM HAPILSILIP AFTAFSLVLL GNPGSGALEH DPRQPWRRGI SFISILLGLA
TAISYFMMAS TGQITVYQLG EWSAPFGIVL VLDRLSAFMV LLTYVLATPV LWFASKEWDA
RGRYFHVMYH FLLMGVCGAF LTGDLFNLFV FFEVLLLASY VLLLHTQGKA RFQLGIHYVT
INLLASALFL IGLGMIYGNV GSLNMADVAR LVPILEPEQH KLAIAGGLLL FVVFGIKAAM
LPVGFWLPKT YAVATTPVAA LFTIMTKVGI YAILRVNGTV FDDDFSQAML QKWLLPIGLV
TSLYGVIGAI GADRLRRFIG FMILSSVGTI LIAIAMSNTQ AWAAALYYLV HSTLIAAAFY
LFSGWITSQR GEFKDHLKIA PQMKQEKITS ITFLVIALML AGLPPFSGFW GKVFILQSSA
QSAYQGWIIA IILIVSLLSI IALTRVGFVL FWRASRPEDN PKEPAYAVYQ ALPDRAPARN
NQTIYVLLAG LILYVVFAAP IQQYTLATAE QIRDRSLYIN QVLKKDREGN VISVASYDPT
YLPETKYGGE ALDSNAHYIP YIISENSLKG EHISPYKQRQ IQQQLNNESV APTDAQLKPM
EP
//
