KDPA_LISMO
ID KDPA_LISMO Reviewed; 561 AA.
AC Q8Y3Z6;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=lmo2682;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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 extracellular 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 membrane {ECO:0000255|HAMAP-Rule:MF_00275};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00275}.
CC -!- SIMILARITY: Belongs to the KdpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
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DR EMBL; AL591984; CAD00895.1; -; Genomic_DNA.
DR PIR; AI1409; AI1409.
DR RefSeq; NP_466204.1; NC_003210.1.
DR RefSeq; WP_003733063.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y3Z6; -.
DR SMR; Q8Y3Z6; -.
DR STRING; 169963.lmo2682; -.
DR PaxDb; Q8Y3Z6; -.
DR EnsemblBacteria; CAD00895; CAD00895; CAD00895.
DR GeneID; 987148; -.
DR KEGG; lmo:lmo2682; -.
DR PATRIC; fig|169963.11.peg.2748; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_9; -.
DR OMA; LMMWTEF; -.
DR PhylomeDB; Q8Y3Z6; -.
DR BioCyc; LMON169963:LMO2682-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
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 membrane; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..561
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166505"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 561 AA; 59315 MW; B161206608500657 CRC64;
MKYIVMQDVF FVVLLLVLAV PLGIYMYKVM IGEKVFLSRV LEPVERFGYR LMGVSEVGMS
AKRYAVSVLA FSAVGFVFVM AVLMLQGFLP LNPEGMKGLS FSLAFNTAAS FVSNTNWQAY
SGETALSYFS QSIGLTVQNF VSAATGIAVL FAVIRGFIWK KQKTVGNFWQ DLFRVTLYIL
LPLSLILALL LVSQGVVQSF ADYSVVETLE NGAKQLIPLG PAASQIAIKQ LGTNGGGFFG
ANSAFPFENP SSFTNLIEML AILLIPVALV VMFGRAVKDS KQGRAIMTAM MIVFVIGVVA
ITISEQFAGP SYQGVATSGS MEGKEVRFGV GGSSLFAAST TAASNGAVNA MHDSLTPLGG
LVPMFFMQLG EVIFGGVGSG LYGMIGFIIL TVFIAGLLVG RTPEYLGKKI EPYDMKMVCL
LILVPPLLTL FGTAVAVMMP SVQASVSASG AHGFSEVLYA FTSMGNNNGS AFAGFAADTT
FTNMVGAVMM LLARFIPLVA ALYLAQNMAG KSSVAASSGT LSTKNGMFIG LLIGVVVLVG
ALSFLPALAL GPIADFFTTF K
