KDPA_SHIB3
ID KDPA_SHIB3 Reviewed; 557 AA.
AC B2TTJ6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=SbBS512_E0551;
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512;
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001063; ACD10322.1; -; Genomic_DNA.
DR RefSeq; WP_000730099.1; NC_010658.1.
DR AlphaFoldDB; B2TTJ6; -.
DR SMR; B2TTJ6; -.
DR STRING; 344609.SbBS512_E0551; -.
DR EnsemblBacteria; ACD10322; ACD10322; SbBS512_E0551.
DR KEGG; sbc:SbBS512_E0551; -.
DR HOGENOM; CLU_018614_3_0_6; -.
DR OMA; RQGWAIL; -.
DR Proteomes; UP000001030; 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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..557
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_1000114706"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 63..83
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 170..190
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 329..349
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 484..504
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 557 AA; 59173 MW; E3587B25C556F2F7 CRC64;
MAAQGFLLIA TFLLVLMVLA RPLGSGLARL INDIPLPGTA GVERILFRLP GVSDHEMNWK
QYLCAILGLN MLGLAVLFFM LLGQHYLPLN PQQLPGLSWD LALNTAVNFV TNTNWQSYSG
ETTLSYFSQM AGLTVQNFLS AASGIAVIFA FIRAFTRQSM STLGNAWVDL LRITLWVLVP
VALLIALFLI QQGALQNFLP YQAVNTVEGA QQLLPMGPVA SQEAIKMLGT NGGGFFNANS
SHPFENPTAL TNFVQMLAIF LIPTALCFAF GEVTGDRRQG RMLLWAMSVI FVICVGVVMW
AEVQGNPHLL ALGADSSINM EGKESRFGVL VSSLFAVVTT AASCGAVIAM HDSFTALGGM
VPMWLMQIGE VVFGGVGSGL YGMMLFVLLA VFIAGLMIGR TPEYLGKKID VREMKLTALA
ILVTPTLVLM GAALAMMTDA GRSAMLNPGP HGFSEVLYAV SSAANNNGSA FAGLSANSPF
WNCLLAFCMF VGRFGVIIPV MAIAGSLVSK KSQPASSGTL PTHGPLFVGL LIGTVLLVGA
LTFIPALALG PVAEYLS