ID Q6F772_ACIAD Unreviewed; 613 AA.
AC Q6F772;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE SubName: Full=Glutathione-regulated potassium-efflux system protein (K(+)/H(+) antiporter) {ECO:0000313|EMBL:CAG70093.1};
GN Name=kef {ECO:0000313|EMBL:CAG70093.1};
GN OrderedLocusNames=ACIAD3441 {ECO:0000313|EMBL:CAG70093.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG70093.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG70093.1, 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|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC transporter (TC 2.A.37) family. {ECO:0000256|ARBA:ARBA00005551}.
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DR EMBL; CR543861; CAG70093.1; -; Genomic_DNA.
DR RefSeq; WP_004923518.1; NC_005966.1.
DR AlphaFoldDB; Q6F772; -.
DR STRING; 202950.GCA_001485005_01763; -.
DR GeneID; 45235626; -.
DR KEGG; aci:ACIAD3441; -.
DR eggNOG; COG0475; Bacteria.
DR eggNOG; COG1226; Bacteria.
DR HOGENOM; CLU_005126_9_3_6; -.
DR OrthoDB; 9781411at2; -.
DR BioCyc; ASP62977:ACIAD_RS15560-MONOMER; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR Gene3D; 1.20.1530.20; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR004771; K/H_exchanger.
DR InterPro; IPR006036; K_uptake_TrkA.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003148; RCK_N.
DR NCBIfam; TIGR00932; 2a37; 1.
DR PANTHER; PTHR46157; K(+) EFFLUX ANTIPORTER 3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR46157:SF4; K(+) EFFLUX ANTIPORTER 3, CHLOROPLASTIC; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02254; TrkA_N; 1.
DR PRINTS; PR00335; KUPTAKETRKA.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51201; RCK_N; 1.
PE 3: Inferred from homology;
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 406..528
FT /note="RCK N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51201"
FT REGION 571..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 66665 MW; 0D6C2C9B35FF00E8 CRC64;
MSEEAHSISL LAPVVLLTAA VIAVPLFKRI GLGSVLGYLI AGLVIGPFGL AFFSDSASIL
HIAELGIVMY LFIIGLEMQP SHLWGLRREI FGLGTFQIVV CALGLTATGM LFGFSWQIAF
IAAAGFVLTS TAIVMQLLGD RGDITQPRGQ KIVAILLFED LLIVPLLAIV AFMAPNQVVE
STTSRFENIG IGLLAIAGLI AAGFWLLNPL FRLLAASKAR EVMTAAALLV VLGAALLMQV
SGLSMAMGAF LAGVLLSEST FRHQIEADIE PFRGILLGLF FLGVGMSLDL KVVAQNWPLI
LSSVVAFMFV KALMIYIVAR TTKSSHQEAL DRALLMAQGG EFAFVLFAAA TSAQVIDSTI
KSNLTAIVVL SMVLTPIIGI LFGRFTKSSK QVSLENVDIA ENLKGNVLLI GFGRFGQVAS
QLLLARGVDV TIIDTDIDMI QNAEKFGFKI YYGDGSRLDI LHASGADQAE AILVCVDQKE
MTNKIVDLVQ HEFPLAKLLV RSYDREHSLY LVKQNVDYIM RETFESAIKF GGAVLEELGV
DEQEIRQITR EIRERDEERY ETEIAADDVY AGGGLQYTNQ HPRPTAPLIQ PKQSAKILND
KDTQDLLDKD EQP
//
