KDPA_BURPS
ID KDPA_BURPS Reviewed; 602 AA.
AC Q63VS3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Potassium-transporting ATPase potassium-binding subunit {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=ATP phosphohydrolase [potassium-transporting] A chain {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=Potassium-binding and translocating subunit A {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=Potassium-translocating ATPase A chain {ECO:0000255|HAMAP-Rule:MF_00275};
GN Name=kdpA {ECO:0000255|HAMAP-Rule:MF_00275}; OrderedLocusNames=BPSL1171;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- FUNCTION: Part of the high-affinity ATP-driven potassium transport (or
CC Kdp) system, which catalyzes the hydrolysis of ATP coupled with the
CC electrogenic transport of potassium into the cytoplasm. This subunit
CC binds the periplasmic potassium ions and delivers the ions to the
CC membrane domain of KdpB through an intramembrane tunnel.
CC {ECO:0000255|HAMAP-Rule:MF_00275}.
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC. {ECO:0000255|HAMAP-Rule:MF_00275}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00275}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
CC -!- SIMILARITY: Belongs to the KdpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
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DR EMBL; BX571965; CAH35166.1; -; Genomic_DNA.
DR RefSeq; WP_004550718.1; NZ_CP009538.1.
DR RefSeq; YP_107793.1; NC_006350.1.
DR AlphaFoldDB; Q63VS3; -.
DR SMR; Q63VS3; -.
DR STRING; 272560.BPSL1171; -.
DR EnsemblBacteria; CAH35166; CAH35166; BPSL1171.
DR KEGG; bps:BPSL1171; -.
DR PATRIC; fig|272560.51.peg.363; -.
DR eggNOG; COG2060; Bacteria.
DR OMA; RQGWAIL; -.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00275; KdpA; 1.
DR InterPro; IPR004623; KdpA.
DR PANTHER; PTHR30607; PTHR30607; 1.
DR Pfam; PF03814; KdpA; 1.
DR PIRSF; PIRSF001294; K_ATPaseA; 1.
DR TIGRFAMs; TIGR00680; kdpA; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..602
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166488"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 602 AA; 62888 MW; 7E090CCDD8466E56 CRC64;
MNANNLLQAA IFIVVLIAAA VPVARYLTRV MDGSSAVVRV FGPLERALYR FAGIDPRTEM
SWKQYALATV AFNALGVLFL YALLRVQGWL PGNPQGFGPM TVDGALNTAV SFVTNTNWQD
YTPEQTVSYL AQMLGLTVQN FLSAATGIVV VLALIRGFAR HTAQTIGNFW VDVTRVTLYV
LVPMAAIIAA LLMSQGVIQN TKAYQDVPTL QTTSYAAPRL DAQGNPVKDA KGNPVTVQTS
VKAQTLAMGP VASQEAIKML GTNGGGFFNG NSSHPYENPT PFSNFLEIFA ILIIPAALCL
VFGNTIGDRR QGVAVLAAMT VALAAAIGIE TSAEQGGTPV LASLNVDLAA SPLQAGGNME
GKETRFGIAQ TGLFVVATTA ASCGAVDAMH DSLTPVGGLV PMLLMQLGEV IFGGVGSGLY
GMLVFALLAV FVAGLMIGRT PEYVGKKIES YEMKMVSIVV LLTPLLVLVG TSIAVLADAG
RAGIANPGPH GFSEILYAFS SAANNNGSAF GGLSVNTPFY NWMTAIAMWF GRFGTIVPVL
AIAGSLAAKK RIAATSGTLP THGPLFVVLL LGTVLLVGAL TYMPALALGP GVEHLMLFVG
AH
