(data stored in SCRATCH zone)

SWISSPROT: B4STF1_STRM5

ID   B4STF1_STRM5            Unreviewed;       216 AA.
AC   B4STF1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Potassium-transporting ATPase KdpC subunit {ECO:0000256|HAMAP-Rule:MF_00276, ECO:0000256|SAAS:SAAS00920423};
DE   AltName: Full=ATP phosphohydrolase [potassium-transporting] C chain {ECO:0000256|HAMAP-Rule:MF_00276};
DE   AltName: Full=Potassium-binding and translocating subunit C {ECO:0000256|HAMAP-Rule:MF_00276};
DE   AltName: Full=Potassium-translocating ATPase C chain {ECO:0000256|HAMAP-Rule:MF_00276};
GN   Name=kdpC {ECO:0000256|HAMAP-Rule:MF_00276};
GN   OrderedLocusNames=Smal_0289 {ECO:0000313|EMBL:ACF49994.1};
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:ACF49994.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49994.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49994.1,
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 acts as a catalytic chaperone that increases the ATP-
CC       binding affinity of the ATP-hydrolyzing subunit KdpB by the
CC       formation of a transient KdpB/KdpC/ATP ternary complex.
CC       {ECO:0000256|HAMAP-Rule:MF_00276, ECO:0000256|SAAS:SAAS00920451}.
CC   -!- SUBUNIT: The system is composed of three essential subunits: KdpA,
CC       KdpB and KdpC. {ECO:0000256|HAMAP-Rule:MF_00276,
CC       ECO:0000256|SAAS:SAAS00920441}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00276}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00276}.
CC   -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00276, ECO:0000256|SAAS:SAAS00920434}.
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DR   EMBL; CP001111; ACF49994.1; -; Genomic_DNA.
DR   RefSeq; WP_012509818.1; NC_011071.1.
DR   STRING; 391008.Smal_0289; -.
DR   EnsemblBacteria; ACF49994; ACF49994; Smal_0289.
DR   KEGG; smt:Smal_0289; -.
DR   eggNOG; ENOG4108R80; Bacteria.
DR   eggNOG; COG2156; LUCA.
DR   HOGENOM; HOG000244124; -.
DR   KO; K01548; -.
DR   OMA; LIAQKFD; -.
DR   OrthoDB; 1912405at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01465-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008556; F:potassium-transporting ATPase activity; IEA:InterPro.
DR   HAMAP; MF_00276; KdpC; 1.
DR   InterPro; IPR003820; KdpC.
DR   PANTHER; PTHR30042; PTHR30042; 1.
DR   Pfam; PF02669; KdpC; 1.
DR   PIRSF; PIRSF001296; K_ATPase_KdpC; 1.
DR   TIGRFAMs; TIGR00681; kdpC; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4STF1.
DR   SWISS-2DPAGE; B4STF1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00276,
KW   ECO:0000256|SAAS:SAAS00920427};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00276};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00276,
KW   ECO:0000256|SAAS:SAAS00920433};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000313|EMBL:ACF49994.1};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_00276,
KW   ECO:0000256|SAAS:SAAS00920454};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00276,
KW   ECO:0000256|SAAS:SAAS00920448};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00276,
KW   ECO:0000256|SAAS:SAAS00920424};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_00276,
KW   ECO:0000256|SAAS:SAAS00920453};
KW   Potassium transport {ECO:0000256|HAMAP-Rule:MF_00276,
KW   ECO:0000256|SAAS:SAAS00920450};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00276,
KW   ECO:0000256|SAAS:SAAS00920430};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00276,
KW   ECO:0000256|SAAS:SAAS00920428};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00276,
KW   ECO:0000256|SAAS:SAAS00920444}.
FT   TRANSMEM     33     60       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00276}.
SQ   SEQUENCE   216 AA;  22164 MW;  3889114B70E79A79 CRC64;
     MNRTASTSSS LPREQKAEAR VASLQDGASW RPAIGLGLAT LLLAGAVYAG IATGFAGLAY
     PTQAEGSLLR DGNGQVRGSA WLSQPFTGDG YFQARPSAAN YDPMAAAGSN LARSNPALAE
     RVAASTAAVA ARESVAPAQV PADLVTQSAG GLDPQLSPAA AQLQVARVAR ARGLPVERVQ
     ALVQAHTEGR QWGLFGQPRV NVVTLNFALD HAAKAP
//

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