KDPA_YERPE
ID KDPA_YERPE Reviewed; 562 AA.
AC Q8ZD96; Q0WDJ8;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 124.
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};
GN OrderedLocusNames=YPO2692, YP_2495;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(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; AL590842; CAL21311.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62694.1; -; Genomic_DNA.
DR PIR; AD0328; AD0328.
DR RefSeq; WP_002209652.1; NZ_WUCM01000006.1.
DR RefSeq; YP_002347640.1; NC_003143.1.
DR AlphaFoldDB; Q8ZD96; -.
DR SMR; Q8ZD96; -.
DR STRING; 214092.YPO2692; -.
DR PaxDb; Q8ZD96; -.
DR EnsemblBacteria; AAS62694; AAS62694; YP_2495.
DR GeneID; 57976001; -.
DR KEGG; ype:YPO2692; -.
DR KEGG; ypm:YP_2495; -.
DR PATRIC; fig|214092.21.peg.3130; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_6; -.
DR OMA; RQGWAIL; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; 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 inner membrane; Cell membrane; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..562
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166539"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 175..195
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 283..303
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 562 AA; 59249 MW; E968731F8121AB42 CRC64;
MVASGFLLIA SFMLVLFVLS RPLGGFLARL IEGEPFSALQ KVEAGLWRCS GVKNAEMNGW
QYALAILCFN LLGIVLLFVL LMTQGSLPLN PEHLPGMSWH LALNTAVSFV TNTNWQAYSG
ENTLSYLSQM AGLTVQNFLS AATGIAVAFA LIRAFARHSA TTLGNAWVDL VRITLYVLLP
IALIIALIFV SQGVLQNLDD YLHITTLEGV QQTLPMGPVA SQEAIKVLGT NGGGFFGANS
AHPFENPTAF SNFVQMLAIF LIPCALCFAF GQVVGDNRQG HALIWAMSLI FIVAVVVVMY
AELAGNPHLS PLGADSNSNM EGKESRFGIL ATSLYAVVTT AASCGAVNAM HDSFTALGGM
IPLWLMQIGE VVFGGVGSGL YGMLLFVLLT VFIAGLMIGR TPEYLGKKID VFDMKMTALA
ILVTPTIVLL GTALALCTEA GRAGILNPGA HGFSEVLYAL SSAANNNGSA FAGLSVNTPF
YNLLLAAAMF IGRFGVILPV LAIASSLVAK KRQPAGNGTL PTGGLLFIGL LIGTVLLVGA
LTFIPALALG PVAEHLQVWL AH