(data stored in SCRATCH zone)

SWISSPROT: B4STF3_STRM5

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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