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Database: UniProt
Entry: H3NJH3_9LACT
LinkDB: H3NJH3_9LACT
Original site: H3NJH3_9LACT 
ID   H3NJH3_9LACT            Unreviewed;       220 AA.
AC   H3NJH3;
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=HMPREF9708_01012 {ECO:0000313|EMBL:EHR36786.1};
OS   Facklamia languida CCUG 37842.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX   NCBI_TaxID=883113 {ECO:0000313|EMBL:EHR36786.1, ECO:0000313|Proteomes:UP000006190};
RN   [1] {ECO:0000313|EMBL:EHR36786.1, ECO:0000313|Proteomes:UP000006190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 37842 {ECO:0000313|EMBL:EHR36786.1,
RC   ECO:0000313|Proteomes:UP000006190};
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 Facklamia languida CCUG 37842.";
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:EHR36786.1}.
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DR   EMBL; AGEG01000013; EHR36786.1; -; Genomic_DNA.
DR   RefSeq; WP_006309147.1; NZ_JH601133.1.
DR   AlphaFoldDB; H3NJH3; -.
DR   STRING; 883113.HMPREF9708_01012; -.
DR   PATRIC; fig|883113.3.peg.1007; -.
DR   eggNOG; COG2156; Bacteria.
DR   HOGENOM; CLU_077094_1_0_9; -.
DR   OrthoDB; 9809491at2; -.
DR   Proteomes; UP000006190; 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:UP000006190};
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        20..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00276"
SQ   SEQUENCE   220 AA;  24370 MW;  11DA8E2051D24808 CRC64;
     MNKKIKTLFH GGRQAFSVSL VLMVICGFLF PILLTGLSAI FFPYQAEGSL LKVKDKAVAS
     ENVGQEFLED YYMWSRPSAY HYNVYTENKE GDKRYQDGSE FPGIASGSNN YAPSNPDLIK
     RVEADMQDFL DKNKGIQPED IPTDLLTASG SGLDPHISPE SARIQIPRIV EASGLSKALV
     QNIIKKHTDE KLLGVMGEES VNVVKVNIEI AKEMGLIQDE
//
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