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KDPC_DEIRA
ID   KDPC_DEIRA              Reviewed;         217 AA.
AC   Q9RZN6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 127.
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=DR_B0087;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OG   Plasmid megaplasmid MP1.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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; AE001826; AAF12537.1; -; Genomic_DNA.
DR   PIR; E75627; E75627.
DR   RefSeq; NP_051620.1; NC_000958.1.
DR   RefSeq; WP_010883955.1; NZ_CP015083.1.
DR   AlphaFoldDB; Q9RZN6; -.
DR   SMR; Q9RZN6; -.
DR   EnsemblBacteria; AAF12537; AAF12537; DR_B0087.
DR   KEGG; dra:DR_B0087; -.
DR   PATRIC; fig|243230.17.peg.85; -.
DR   HOGENOM; CLU_077094_2_0_0; -.
DR   InParanoid; Q9RZN6; -.
DR   OMA; KYFWPRP; -.
DR   OrthoDB; 1912405at2; -.
DR   BRENDA; 7.2.2.6; 1856.
DR   Proteomes; UP000002524; Plasmid megaplasmid MP1.
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; IBA:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
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   Plasmid; Potassium; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..217
FT                   /note="Potassium-transporting ATPase KdpC subunit"
FT                   /id="PRO_0000196989"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
FT   REGION          87..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   217 AA;  22329 MW;  1BFC95958D64EDC5 CRC64;
     MTTPNANLQN SAPLPAERPT PLPRLLLSAL LAAVLFMLVC GLAYPLLTTV VAGAAFPNQA
     GGSLVTRNGQ VVGSAVLGQN FTAPRYLHGR PSMTSKTDGS GPEPYNAENS GASNWGPTNA
     KLQGAVQGRI AAFRQENGLG ADVPVPIDAV TASASGLDPD VTLATALLQV NRIAQARGMQ
     PAGVEKVIRA HLKGRDLGLL GEPRVNVLAV NLSLDGQ
 
 
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