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Database: UniProt
Entry: H3NLX6_9FIRM
LinkDB: H3NLX6_9FIRM
Original site: H3NLX6_9FIRM 
ID   H3NLX6_9FIRM            Unreviewed;       216 AA.
AC   H3NLX6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   ORFNames=HMPREF9709_00337 {ECO:0000313|EMBL:EHR35646.1};
OS   Helcococcus kunzii ATCC 51366.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Helcococcus.
OX   NCBI_TaxID=883114 {ECO:0000313|EMBL:EHR35646.1, ECO:0000313|Proteomes:UP000004191};
RN   [1] {ECO:0000313|EMBL:EHR35646.1, ECO:0000313|Proteomes:UP000004191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51366 {ECO:0000313|EMBL:EHR35646.1,
RC   ECO:0000313|Proteomes:UP000004191};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Helcococcus kunzii ATCC 51366.";
RL   Submitted (JAN-2012) 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: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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHR35646.1}.
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DR   EMBL; AGEI01000011; EHR35646.1; -; Genomic_DNA.
DR   RefSeq; WP_005397337.1; NZ_JH601088.1.
DR   AlphaFoldDB; H3NLX6; -.
DR   STRING; 883114.HMPREF9709_00337; -.
DR   PATRIC; fig|883114.3.peg.331; -.
DR   eggNOG; COG2156; Bacteria.
DR   HOGENOM; CLU_077094_1_0_9; -.
DR   OrthoDB; 9809491at2; -.
DR   Proteomes; UP000004191; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; 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   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};
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:UP000004191};
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}.
SQ   SEQUENCE   216 AA;  23815 MW;  206CED38A12C0AC2 CRC64;
     MKNSKNIFSS LRQSFLITFV LMIICGLLFP LVLTGMSSVL FAEKANGSII DINDKKYGSK
     IVGQEFKENY YMWSRPSSVK YDIFIEDNNG NQTYTNGEKF NGVSSGSQNL APSNPDLAKR
     VEEGMTAFLK ANPDVKQSEI PADLLTASGS GLDPHISYQS ALIQISRIVK YSGLDEAKIK
     SIVEKNTENK LFGVFGEKVV NVLGVNIDIA KEINKL
//
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