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KDPC_STAHJ
ID   KDPC_STAHJ              Reviewed;         185 AA.
AC   Q4LAI1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Potassium-transporting ATPase KdpC subunit {ECO:0000255|HAMAP-Rule:MF_00276};
DE   AltName: Full=ATP phosphohydrolase [potassium-transporting] C chain {ECO:0000255|HAMAP-Rule:MF_00276};
DE   AltName: Full=Potassium-binding and translocating subunit C {ECO:0000255|HAMAP-Rule:MF_00276};
DE   AltName: Full=Potassium-translocating ATPase C chain {ECO:0000255|HAMAP-Rule:MF_00276};
GN   Name=kdpC {ECO:0000255|HAMAP-Rule:MF_00276}; OrderedLocusNames=SH0035;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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       acts as a catalytic chaperone that increases the ATP-binding affinity
CC       of the ATP-hydrolyzing subunit KdpB by the formation of a transient
CC       KdpB/KdpC/ATP ternary complex. {ECO:0000255|HAMAP-Rule:MF_00276}.
CC   -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC       and KdpC. {ECO:0000255|HAMAP-Rule:MF_00276}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00276};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00276}.
CC   -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00276}.
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DR   EMBL; AP006716; BAE03344.1; -; Genomic_DNA.
DR   RefSeq; WP_011274390.1; NC_007168.1.
DR   AlphaFoldDB; Q4LAI1; -.
DR   SMR; Q4LAI1; -.
DR   STRING; 279808.SH0035; -.
DR   EnsemblBacteria; BAE03344; BAE03344; SH0035.
DR   KEGG; sha:SH0035; -.
DR   eggNOG; COG2156; Bacteria.
DR   HOGENOM; CLU_077094_2_0_9; -.
DR   OMA; PDLKWFQ; -.
DR   OrthoDB; 1912405at2; -.
DR   Proteomes; UP000000543; 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:P-type potassium transmembrane transporter 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;
KW   ATP-binding; Cell membrane; Ion transport; Membrane; Nucleotide-binding;
KW   Potassium; Potassium transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..185
FT                   /note="Potassium-transporting ATPase KdpC subunit"
FT                   /id="PRO_0000197018"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
FT   REGION          113..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   185 AA;  20136 MW;  C5307020FE5083F0 CRC64;
     MQTIRKSLGL VLIMFVLCGF IFPLTVTALG QVLFPEQANG SLVKQDGKVI GSKLIGQQWT
     EPKYFHGRIS AVNYNMNANE VKESGGPASG GSNYGNSNPE LKKRVQETIK QEGQKLSSDA
     VTTSGSGLDP DITVDNAKQQ VKCIAKERNI DASKINHLID ENKQASPMAD DYVNVLKLNI
     TLDKL
 
 
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