KDPA_STAAS
ID KDPA_STAAS Reviewed; 558 AA.
AC Q6G7N2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, 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=SAS1982;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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 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; BX571857; CAG43789.1; -; Genomic_DNA.
DR RefSeq; WP_000402658.1; NC_002953.3.
DR AlphaFoldDB; Q6G7N2; -.
DR SMR; Q6G7N2; -.
DR KEGG; sas:SAS1982; -.
DR HOGENOM; CLU_018614_3_0_9; -.
DR OMA; RQGWAIL; -.
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 membrane; Ion transport; Membrane; Potassium; Potassium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..558
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166531"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 281..301
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 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 377..397
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 482..502
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 558 AA; 62042 MW; 0E27E1F4B50B3DAA CRC64;
MEIILFLTMM VMITYVFSGY LYRVALVQSS RVDLIFTRFE NMCFKIIGTD LEHMSAKTYV
KHFLAFNGFM GFITFVLLIV QQWLFLNPNH NLNQSIDLAF NTAISFLTNS NLQHYNGESD
VTYLTQMIVM TYLMFTSSAS GYAVCIAMLR RLTGLTNIIG NFYQDIVRFI VRVLLPLSCL
ISILLMTQGV PQTLHANLMI RTLSGHIQHI AFGPIASLES IKHLGTNGGG FLAGNSATPF
ENPNIWSNFI EMGSMMLLPM SMLFLFGRML SRHGKRVHRH ALILFVAMFF IFIAILTLTM
WSEYRGNPIL ANLGIYGPNM EGKEVRFGAG LSALFTVITT AFTTGSVNNM HDSLTPLGGL
GPMVLMMLNV VFGGEGVGLM NLLIYVLLTV FICSLMVGKT PEYLNMPIGA REMKCIVLVF
LIHPILILVF SALAFMIPGA SESITNPSFH GISQVMYEMT SAAANNGSGF EGLKDDTTFW
NISTGIIMLL SRYIPIILQL MIASSLVNKK SYHQDKYTIA IDKPYFGVSL IVFIVLLSGL
TFIPVLLLGP IGEFLTLK
