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Database: UniProt
Entry: A0A0A7G1G2_9CLOT
LinkDB: A0A0A7G1G2_9CLOT
Original site: A0A0A7G1G2_9CLOT 
ID   A0A0A7G1G2_9CLOT        Unreviewed;       198 AA.
AC   A0A0A7G1G2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Potassium-transporting ATPase KdpC subunit {ECO:0000256|HAMAP-Rule:MF_00276};
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   ECO:0000313|EMBL:AIY84801.1};
GN   ORFNames=U729_175 {ECO:0000313|EMBL:AIY84801.1};
OS   Clostridium baratii str. Sullivan.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY84801.1, ECO:0000313|Proteomes:UP000030635};
RN   [1] {ECO:0000313|EMBL:AIY84801.1, ECO:0000313|Proteomes:UP000030635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sullivan {ECO:0000313|EMBL:AIY84801.1};
RX   PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA   Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA   Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA   Karavis M.A., Smith L.A.;
RT   "Genomic sequences of six botulinum neurotoxin-producing strains
RT   representing three clostridial species illustrate the mobility and
RT   diversity of botulinum neurotoxin genes.";
RL   Infect. Genet. Evol. 30:102-113(2014).
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:0000256|HAMAP-Rule:MF_00276}.
CC   -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC       and KdpC. {ECO:0000256|HAMAP-Rule:MF_00276}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00276};
CC       Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00276}.
CC   -!- SIMILARITY: Belongs to the KdpC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00276}.
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DR   EMBL; CP006905; AIY84801.1; -; Genomic_DNA.
DR   RefSeq; WP_039310864.1; NZ_CP006905.1.
DR   AlphaFoldDB; A0A0A7G1G2; -.
DR   STRING; 1561.NPD11_2800; -.
DR   KEGG; cbv:U729_175; -.
DR   eggNOG; COG2156; Bacteria.
DR   HOGENOM; CLU_077094_1_0_9; -.
DR   OrthoDB; 9809491at2; -.
DR   Proteomes; UP000030635; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro.
DR   HAMAP; MF_00276; KdpC; 1.
DR   InterPro; IPR003820; KdpC.
DR   NCBIfam; TIGR00681; kdpC; 1.
DR   PANTHER; PTHR30042; POTASSIUM-TRANSPORTING ATPASE C CHAIN; 1.
DR   PANTHER; PTHR30042:SF2; POTASSIUM-TRANSPORTING ATPASE KDPC SUBUNIT; 1.
DR   Pfam; PF02669; KdpC; 1.
DR   PIRSF; PIRSF001296; K_ATPase_KdpC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00276};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00276}; Hydrolase {ECO:0000313|EMBL:AIY84801.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_00276};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00276};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00276};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00276};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538, ECO:0000256|HAMAP-
KW   Rule:MF_00276}; Reference proteome {ECO:0000313|Proteomes:UP000030635};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00276};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00276};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00276}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00276"
SQ   SEQUENCE   198 AA;  22074 MW;  E1BA13D5DB4B8028 CRC64;
     MRYFNKGLRI TVSMIIICGI IYPLLITGIG QLFFNYEANG SVMEVDGKEV GSELIGQIYN
     EEKYFNGRVS AVNYNISDDG KEIDSTSGSQ NLGPTSEVLK ERVEKDIENF LKKNPTVSRD
     EITEELISQS GSGLDPHITV RGAEIQIDRI SKVTGISKDR LKMLIEENKE GKLLGLYGAE
     RVNVLKLNIG IDKILKEE
//
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