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KDPA_CLOP1
ID   KDPA_CLOP1              Reviewed;         578 AA.
AC   Q0TRT4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-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=CPF_1210;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(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 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; CP000246; ABG83847.1; -; Genomic_DNA.
DR   RefSeq; WP_003456394.1; NC_008261.1.
DR   AlphaFoldDB; Q0TRT4; -.
DR   SMR; Q0TRT4; -.
DR   STRING; 195103.CPF_1210; -.
DR   PRIDE; Q0TRT4; -.
DR   EnsemblBacteria; ABG83847; ABG83847; CPF_1210.
DR   GeneID; 29571674; -.
DR   KEGG; cpf:CPF_1210; -.
DR   eggNOG; COG2060; Bacteria.
DR   HOGENOM; CLU_018614_3_0_9; -.
DR   OMA; LMMWTEF; -.
DR   OrthoDB; 296671at2; -.
DR   Proteomes; UP000001823; 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   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..578
FT                   /note="Potassium-transporting ATPase potassium-binding
FT                   subunit"
FT                   /id="PRO_1000022217"
FT   TRANSMEM        3..23
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        134..154
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        261..281
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        397..417
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        543..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ   SEQUENCE   578 AA;  61786 MW;  824DA7EC4E18C0CD CRC64;
     MSNAILQYSL YLIILVLLAI PLGKYIGKVM NEEKVFLSKL ILPCENFIYK VLGINEEDMD
     WKKYSFSVLA FSAVGFIFLF ALNLLQGVLP LNPEGISGSS WDLSFNTTAS FITNTNWQAY
     SGESQLSYLT QMLGLTVQNF LSAGVGIAVL FALIRGFTRV NKSGLGNFWR DLTRIVLYLL
     VPLSIVLSIL LVSQGTVQNF KPYEEVALLE EIVLDDGNRV TSQIVPQGPA ASQVAIKQLG
     TNGGGFFGVN SAHPLENPTA FSNLLEMLSI LLIPAALCFT FGRNIKDKRQ GRAIFIAMFT
     LLIIALCIIG VSEANGTPQL AQNGDVNLGY IDQSGGNMEG KESRFGVVGS STWAAFTTAA
     SNGSVNSMHD SFTPIGGMVT MLLMQLGEVV FGGVGCGLYG MIAFAIITVF IAGLMVGRTP
     EYLGKKIEPY EMKMAMLICL ATPISILIGS ALASINPEIL NSLTNSGAHG FSEILYAYSS
     AGGNNGSAFA GLGANTVFIN VSIGLIMLFV RFVPMIATLA IAGSLVKKKK VATSVGTLPT
     HNLLFIGLLI FVVLLVGALS FFPALALGPI AEFLQMIA
 
 
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