(data stored in ACNUC7421 zone)

SWISSPROT: KDPC_RHOPS

ID   KDPC_RHOPS              Reviewed;         201 AA.
AC   Q13DD7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 79.
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=RPD_0664;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00276}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00276}.
CC   -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00276}.
DR   EMBL; CP000283; ABE37902.1; -; Genomic_DNA.
DR   RefSeq; WP_011501089.1; NC_007958.1.
DR   SMR; Q13DD7; -.
DR   STRING; 316057.RPD_0664; -.
DR   EnsemblBacteria; ABE37902; ABE37902; RPD_0664.
DR   KEGG; rpd:RPD_0664; -.
DR   eggNOG; ENOG4108R80; Bacteria.
DR   eggNOG; COG2156; LUCA.
DR   HOGENOM; HOG000244124; -.
DR   KO; K01548; -.
DR   OMA; FTDARYF; -.
DR   OrthoDB; 1912405at2; -.
DR   BioCyc; RPAL316057:RPD_RS03395-MONOMER; -.
DR   Proteomes; UP000001818; 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 transmembrane transporter activity, phosphorylative mechanism; 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; Q13DD7.
DR   SWISS-2DPAGE; Q13DD7.
KW   ATP-binding; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW   Nucleotide-binding; Potassium; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..201
FT                   /note="Potassium-transporting ATPase KdpC subunit"
FT                   /id="PRO_1000022308"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ   SEQUENCE   201 AA;  20829 MW;  86162DB3481B5C9C CRC64;
     MLKEIRPALV VLVVLTVICG LAYPLAMTGI AGVLFPEQAA GSLIVKDGAV IGSALIGQEF
     KDDKYFHGRP SATSAADPAD PTKTVSSPYN AANSSGSNLG PTSKALNDRV KEDVDKLKAE
     NPSAAVPVDL VTASGSGLDP EISPEAALFQ VPRVARARGL SEDGVRKLVN AQTKGRFAGL
     LGEPRVNVLA LNLALDATTR K
//

If you have problems or comments...

PBIL Back to PBIL home page