KDPA_BORA1
ID KDPA_BORA1 Reviewed; 594 AA.
AC Q2KWC8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=BAV2701;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ50312.1; -; Genomic_DNA.
DR RefSeq; WP_012418343.1; NC_010645.1.
DR AlphaFoldDB; Q2KWC8; -.
DR SMR; Q2KWC8; -.
DR STRING; 360910.BAV2701; -.
DR EnsemblBacteria; CAJ50312; CAJ50312; BAV2701.
DR GeneID; 41394536; -.
DR KEGG; bav:BAV2701; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_4; -.
DR OMA; RQGWAIL; -.
DR OrthoDB; 296671at2; -.
DR Proteomes; UP000001977; Chromosome.
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..594
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_1000022214"
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 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 594 AA; 62631 MW; 06DE90F26B08F54F CRC64;
MDSQFFGLLV FYLAILLILA PFLGRYIRRA MEDEHYAATA WGRWLERLMY RLSGVNPAAE
MTWRQYAVAV LIFSVLGFIA VYALQRLQGF LPLNPVGLGA VSPDSAFNTA ISFVSNTNWQ
GYSPESTMSY LTQMLALTVQ NFLSAAVGMS VLFALIRGFA RHGCATVGNF WVDATRATLY
VLLPLALALA LALVSQGVIQ NTAAYQEVTT LQAQSYEQAR LDSTGQPMMD AAGKPLTETL
VIQTQTLAMG PTASQEAIKL LGINGGGFFN ANSAHPYENP TGLSNLLEML AILIIPAALC
FTFGEMVGDR RQGVAILAAM TLLFVGLAWL TQNAEQALTP ALSHLSADGL LGNMEGKESR
FGVAASALFA VVTTAASCGA VNTMHDSLSA MGGLGPMLLM QLGEVVFGGV GSGLYGMLAF
ALLGVFIAGL MIGRTPEYLG KKIEAFDMKM VSIAILVTPF LVLAGTALAV SVPQGLAGML
NPGAHGFSEV LYALSSAANN NGSAFAGLSS NTPFYNSLLG LAMWFGRFLV IVAILALAGS
LAGKRRLAQS PGSMPTTGPL FIVLLIGTVL LVGALTYVPA LALGPVAEHL QARP
