ID   KDPC2_STAAM             Reviewed;         185 AA.
AC   P0A059; Q932L1; Q9LC48;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Potassium-transporting ATPase KdpC subunit 2 {ECO:0000255|HAMAP-Rule:MF_00276};
DE   AltName: Full=ATP phosphohydrolase [potassium-transporting] C chain 2 {ECO:0000255|HAMAP-Rule:MF_00276};
DE   AltName: Full=Potassium-binding and translocating subunit C 2 {ECO:0000255|HAMAP-Rule:MF_00276};
DE   AltName: Full=Potassium-translocating ATPase C chain 2 {ECO:0000255|HAMAP-Rule:MF_00276};
GN   Name=kdpC2 {ECO:0000255|HAMAP-Rule:MF_00276}; OrderedLocusNames=SAV0074;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=20713508; DOI=10.1101/gad.1945010;
RA   Lopez D., Kolter R.;
RT   "Functional microdomains in bacterial membranes.";
RL   Genes Dev. 24:1893-1902(2010).
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       ECO:0000269|PubMed:20713508}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00276}. Membrane raft
CC       {ECO:0000269|PubMed:20713508}; Single-pass membrane protein
CC       {ECO:0000255}. Note=Present in detergent-resistant membrane (DRM)
CC       fractions that may be equivalent to eukaryotic membrane rafts; these
CC       rafts include proteins involved in signaling, molecule trafficking and
CC       protein secretion. {ECO:0000269|PubMed:20713508}.
CC   -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00276}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB56236.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000017; BAB56236.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001193482.1; NC_002758.2.
DR   AlphaFoldDB; P0A059; -.
DR   SMR; P0A059; -.
DR   PaxDb; P0A059; -.
DR   EnsemblBacteria; BAB56236; BAB56236; SAV0074.
DR   KEGG; sav:SAV0074; -.
DR   HOGENOM; CLU_077094_2_0_9; -.
DR   OMA; PDLKWFQ; -.
DR   BioCyc; SAUR158878:SAV_RS00500-MON; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
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 2"
FT                   /id="PRO_0000197014"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00276"
SQ   SEQUENCE   185 AA;  20159 MW;  5F8B45FB1812E180 CRC64;
     MQTIRKSLGL VLIMFVLCGF IFPLTVTALG QVLFPEQANG SLVKQDGKVI GSKLIGQQWT
     EPKYFHGRIS AVNYNMNANE VKESGGPASG GSNYGNSNPE LKKRVQETIK QEGKKISSDA
     VTASGSGLDP DITVDNAKQQ VKRIAKERNI DASKINHLID ENKQASPMAD DYVNVLKLNI
     TLDKL