(data stored in SCRATCH zone)

SWISSPROT: A8KYG3_FRASN

ID   A8KYG3_FRASN            Unreviewed;       569 AA.
AC   A8KYG3;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   16-JAN-2019, entry version 68.
DE   RecName: Full=Potassium-transporting ATPase potassium-binding subunit {ECO:0000256|HAMAP-Rule:MF_00275};
DE   AltName: Full=ATP phosphohydrolase [potassium-transporting] A chain {ECO:0000256|HAMAP-Rule:MF_00275};
DE   AltName: Full=Potassium-binding and translocating subunit A {ECO:0000256|HAMAP-Rule:MF_00275};
DE   AltName: Full=Potassium-translocating ATPase A chain {ECO:0000256|HAMAP-Rule:MF_00275};
GN   Name=kdpA {ECO:0000256|HAMAP-Rule:MF_00275};
GN   OrderedLocusNames=Franean1_0600 {ECO:0000313|EMBL:ABW10059.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW10059.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- FUNCTION: Part of the high-affinity ATP-driven potassium transport
CC       (or Kdp) system, which catalyzes the hydrolysis of ATP coupled
CC       with the electrogenic transport of potassium into the cytoplasm.
CC       This subunit binds and transports the potassium across the
CC       cytoplasmic membrane. {ECO:0000256|HAMAP-Rule:MF_00275,
CC       ECO:0000256|SAAS:SAAS00682234}.
CC   -!- SUBUNIT: The system is composed of three essential subunits: KdpA,
CC       KdpB and KdpC. {ECO:0000256|HAMAP-Rule:MF_00275,
CC       ECO:0000256|SAAS:SAAS00682238}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00275}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00275}.
CC   -!- SIMILARITY: Belongs to the KdpA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00275, ECO:0000256|SAAS:SAAS00682235}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00275}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000820; ABW10059.1; -; Genomic_DNA.
DR   RefSeq; WP_020458252.1; NC_009921.1.
DR   STRING; 298653.Franean1_0600; -.
DR   EnsemblBacteria; ABW10059; ABW10059; Franean1_0600.
DR   KEGG; fre:Franean1_0600; -.
DR   eggNOG; ENOG4105D9K; Bacteria.
DR   eggNOG; COG2060; LUCA.
DR   HOGENOM; HOG000244102; -.
DR   KO; K01546; -.
DR   OMA; WQNYGGE; -.
DR   OrthoDB; 296671at2; -.
DR   BioCyc; FSP298653:G1G9X-598-MONOMER; -.
DR   Proteomes; UP000001313; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008556; F:potassium-transporting ATPase activity; IEA:InterPro.
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;
DR   PRODOM; A8KYG3.
DR   SWISS-2DPAGE; A8KYG3.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00275,
KW   ECO:0000256|SAAS:SAAS00682233};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
KW   Hydrolase {ECO:0000313|EMBL:ABW10059.1};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_00275,
KW   ECO:0000256|SAAS:SAAS00682246};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00275,
KW   ECO:0000256|SAAS:SAAS00682240};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_00275,
KW   ECO:0000256|SAAS:SAAS00682250};
KW   Potassium transport {ECO:0000256|HAMAP-Rule:MF_00275,
KW   ECO:0000256|SAAS:SAAS00682245};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00275,
KW   ECO:0000256|SAAS:SAAS00682237};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00275,
KW   ECO:0000256|SAAS:SAAS00682236};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00275,
KW   ECO:0000256|SAAS:SAAS00682241}.
FT   TRANSMEM     61     80       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00275}.
FT   TRANSMEM    129    151       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00275}.
FT   TRANSMEM    192    210       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00275}.
FT   TRANSMEM    271    289       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00275}.
FT   TRANSMEM    296    316       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00275}.
FT   TRANSMEM    392    410       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00275}.
FT   TRANSMEM    431    450       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00275}.
FT   TRANSMEM    496    519       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00275}.
FT   TRANSMEM    539    560       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00275}.
SQ   SEQUENCE   569 AA;  59542 MW;  8D4A31D7F55CBB35 CRC64;
     MSMTVAGILV ALLLVGALAT TYRPFGDYMF RVYTSEKHLP VERAIYRLTG VNPNAGQRWT
     VYARSVLAFS AVSVLFLYLL QRVQDHLPWD LGFSGVSPAL AWNTAVSFTT NTDWQAYSGE
     STMSHFTQMA GLAVQNFASA AVGIAVAIAV VRGFARRRAP VAAGPGSMDG VVGTGDEIGN
     FWVDLTRTIV RILLPICVLG AIVLIAGGAI QNLHGNHVVT TVAGGRQAIT GGPVASQEVI
     KELGTNGGGF YNVNSAHPFE NPATWTNLFE IYLLLMIGFS LPRTFGRLVG DRRQGLAIVA
     VMALIALGSL TVNMAFQVAH HGTVPEAVGA AAEGTDARFG VANSAIFATA TTLTSTGAVN
     SFHDSYTSLG GASLLFNMML GEVAPGGVGS GLYGMLVLAV VTVFVAGLMI GRTPEYVGKK
     IGAREMKFAS LYFLTTPIIV LLGTGVAMAL PGQRAGMLNS GAHGLSEVLY SFTSAGNNNG
     SAFAGITVNT TWYNTALGLA MMFGRFLPII FVLGLAGSLA RQTPVPVTAG TLPTHRPQFV
     GMLAGVTLII VALTFFPALA LGPFAEGIH
//

If you have problems or comments...

PBIL Back to PBIL home page