ID   KDPA_DESDA              Reviewed;         583 AA.
AC   B8J1E9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Potassium-transporting ATPase potassium-binding subunit {ECO:0000255|HAMAP-Rule:MF_00275};
DE   AltName: Full=ATP phosphohydrolase [potassium-transporting] A chain {ECO:0000255|HAMAP-Rule:MF_00275};
DE   AltName: Full=Potassium-binding and translocating subunit A {ECO:0000255|HAMAP-Rule:MF_00275};
DE   AltName: Full=Potassium-translocating ATPase A chain {ECO:0000255|HAMAP-Rule:MF_00275};
GN   Name=kdpA {ECO:0000255|HAMAP-Rule:MF_00275}; OrderedLocusNames=Ddes_1677;
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 / DSM 6949 / MB;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT   ATCC 27774.";
RL   Submitted (JAN-2009) 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       binds the periplasmic potassium ions and delivers the ions to the
CC       membrane domain of KdpB through an intramembrane tunnel.
CC       {ECO:0000255|HAMAP-Rule:MF_00275}.
CC   -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC       and KdpC. {ECO:0000255|HAMAP-Rule:MF_00275}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00275}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00275}.
CC   -!- SIMILARITY: Belongs to the KdpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00275}.
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DR   EMBL; CP001358; ACL49576.1; -; Genomic_DNA.
DR   RefSeq; WP_012625300.1; NC_011883.1.
DR   AlphaFoldDB; B8J1E9; -.
DR   SMR; B8J1E9; -.
DR   STRING; 525146.Ddes_1677; -.
DR   EnsemblBacteria; ACL49576; ACL49576; Ddes_1677.
DR   KEGG; dds:Ddes_1677; -.
DR   eggNOG; COG2060; Bacteria.
DR   HOGENOM; CLU_018614_3_0_7; -.
DR   OMA; RQGWAIL; -.
DR   OrthoDB; 296671at2; -.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00275; KdpA; 1.
DR   InterPro; IPR004623; KdpA.
DR   PANTHER; PTHR30607; PTHR30607; 1.
DR   Pfam; PF03814; KdpA; 1.
DR   PIRSF; PIRSF001294; K_ATPaseA; 1.
DR   TIGRFAMs; TIGR00680; kdpA; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Ion transport; Membrane; Potassium;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..583
FT                   /note="Potassium-transporting ATPase potassium-binding
FT                   subunit"
FT                   /id="PRO_1000190734"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        440..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        506..526
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        549..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ   SEQUENCE   583 AA;  61061 MW;  6D1DBF70168F6AB4 CRC64;
     MENIIWQCLL YLSLLTALAW PLGKYIGKVM DGEPFWLQRA LAPCERALYR LMGVDPAEQM
     GWKCYMACVI AFSAVSLVAL TALLMAQHLL PLNPRNVSGA SWHLALNTAI SFVTNTNWQS
     YAGESTMSYL SQMAGLTVQN FVSAAVGIAV LFALIRGVRA SGGIGLGNFW ADATRAVLYI
     LLPLSLVMSL LLIEQGVPQN FTDYRAAALL EPLAAEDGAP ITHQLVPMGP QASQVSPKQL
     GTNGGGFNGV NSAHPHENPT PASNMLEMLA LLLIPAALCF TFGAKIGDMR QGVAIFAAMF
     ILLTSAVSFT VQAELNATPQ IAQGGQVLVA PQSGLQGQAG GNMEGKETRF GIAGSALWAS
     ATTAVSNGSV NAMHDSFTPL GGMIPMVLMQ LGEVIFGGVG SGLYGMLAFV LLTVFLAGLM
     VGRTPEYLGK KIEPFEMKMA VVVCLTTPVV ILAGGGLMCL APQIVDSLNN PLPHGFSEIL
     YAATSAGANN GSAFAGLNAN TPFLNVLLGV LMLAGRFAPI AAILAMADGL AGKKICPPGA
     GTLSTCNGLF IFLLIFVILL VGALSFFPAL ALGPLAEHLQ MTR