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ID B4STF3_STRM5 Unreviewed; 569 AA.
AC B4STF3;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 08-MAY-2019, entry version 69.
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=Smal_0291 {ECO:0000313|EMBL:ACF49996.1};
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas;
OC Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49996.1, ECO:0000313|Proteomes:UP000001867};
RN [1] {ECO:0000313|EMBL:ACF49996.1, ECO:0000313|Proteomes:UP000001867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3 {ECO:0000313|EMBL:ACF49996.1,
RC ECO:0000313|Proteomes:UP000001867};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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 inner 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}.
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DR EMBL; CP001111; ACF49996.1; -; Genomic_DNA.
DR RefSeq; WP_012509820.1; NC_011071.1.
DR STRING; 391008.Smal_0291; -.
DR EnsemblBacteria; ACF49996; ACF49996; Smal_0291.
DR KEGG; smt:Smal_0291; -.
DR eggNOG; ENOG4105D9K; Bacteria.
DR eggNOG; COG2060; LUCA.
DR HOGENOM; HOG000244102; -.
DR KO; K01546; -.
DR OMA; ALMMWTE; -.
DR OrthoDB; 296671at2; -.
DR BioCyc; SMAL391008:SMAL_RS01475-MONOMER; -.
DR Proteomes; UP000001867; 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; B4STF3.
DR SWISS-2DPAGE; B4STF3.
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00275};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00275,
KW ECO:0000256|SAAS:SAAS00682233};
KW Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW Hydrolase {ECO:0000313|EMBL:ACF49996.1};
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 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 6 23 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00275}.
FT TRANSMEM 61 86 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00275}.
FT TRANSMEM 134 155 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00275}.
FT TRANSMEM 176 200 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00275}.
FT TRANSMEM 269 288 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00275}.
FT TRANSMEM 295 316 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00275}.
FT TRANSMEM 380 405 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00275}.
FT TRANSMEM 425 447 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00275}.
FT TRANSMEM 487 513 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00275}.
FT TRANSMEM 534 561 Helical. {ECO:0000256|HAMAP-Rule:
FT MF_00275}.
SQ SEQUENCE 569 AA; 60465 MW; 60B2A5E8C2394A2C CRC64;
MTEIIVILAA SLLLAWPLGL YLARVMRGAP MKVDVLFHWI EKPLYRVFGV DPSRSMSWRG
YVLAFVLSNV VVAVLTQAVF MTQAWLPLNP DQIPNMRWDT ALHTMISFLT NTNQQHYSGQ
AQLSYLSQMT GITGLQVVTP MMGLALAVAT LRALFARSSQ AAAASGAGDD RQVAVGNYYV
DVVRLCVRFL LPLCLVWTLL LTSQGVPSTM AGGPQATPID ASAGMAEQKL PLGPVAAMVA
AKQLGANGGG WYGPNSSFPL ENPTPVSNAL EILGILLVPM SVIFMIGAFT GRRRFGVLVF
SCMLGMSLLS TGAMVWSEGH SPSAATPLLM EGKEVRFGAD GTALWAAVTT QVSNGSVNGM
HDSLAPLSGG IAMVNMLVSA IWGGIGCGLQ QFIVYLLLGV FLAGLMTGRT PELFGRKLET
PQVRLLALLV LLQPITLLVF TAITLAVPGL AGTSNPGFHG ISQVFYEYVS AYANNGSGFE
GLGDATLWWN LSCSLVLLLG RFPLLIIPLV VAAQLAAKRQ SPESAGSLQI ETPTFALTLV
SVIVILTVLQ FMPALVLGPI ADHLSLGLH
//
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