KDPA_HERA2
ID KDPA_HERA2 Reviewed; 579 AA.
AC A9AXU9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=Haur_2275;
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC Herpetosiphon.
OX NCBI_TaxID=316274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) 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 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; CP000875; ABX04915.1; -; Genomic_DNA.
DR AlphaFoldDB; A9AXU9; -.
DR SMR; A9AXU9; -.
DR STRING; 316274.Haur_2275; -.
DR EnsemblBacteria; ABX04915; ABX04915; Haur_2275.
DR KEGG; hau:Haur_2275; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_0; -.
DR OMA; RQGWAIL; -.
DR Proteomes; UP000000787; 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 membrane; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..579
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_1000114686"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 579 AA; 61120 MW; BA664BA011494719 CRC64;
MISNSVIQIG IFLVVLMACV VPLGRYMAKV YGENPPLQGF FGPIERLIYR LLGIDAKSEM
HWKHYALALL GFNAMGMLLL YGLQRMQAWL PLNPQQLPAV SADSAFNTAA SFVSNTNWQG
YAGETTMSYL TQMLGLTVQN FVSAATGMAV LIGLIRGIAR RSTSTIGNFW VDLTRSTIYI
LLPLALVLSV TLVSQGVVQT FSPSQTVELI QPIVNADGTT ISQQTIALGP AASQIAIKQL
GTNGGGFFNV NSAHPLENPT PLSNFLELLS ILLIPAALCY TFGLMVGDKR QGWAILATMT
IILLGFTVLA VSAEQAGNPL YQKLGVDDQA SALQAGGNLE GKETRFGIVN SALWATVTTA
ASNGSVNSMH DSYTPLGGLA PMVLMQLGEV VFGGVGSGLY GMLIFAIIAV FVAGLMVGRT
PEYLGKKIEA FEMKMAALII LIPCVMTLLI TAIAVSSESG RATVFNSGAH GFSEVLYAAT
SAANNNGSAF AGLGANTPFY NTWLGIAMLV SRFWLIVPTL AIAGSLAGKK LIPQSAGTLP
THTPLFVSLL IGVVLIVGAL TFIPALALGP IVEHLLLSL