ID   KDPA_SOLM1              Reviewed;         582 AA.
AC   C4XKM8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=DMR_09290;
OS   Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS   (Desulfovibrio magneticus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Solidesulfovibrio.
OX   NCBI_TaxID=573370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX   PubMed=19675025; DOI=10.1101/gr.088906.108;
RA   Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA   Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA   Matsunaga T.;
RT   "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT   common gene clusters in magnetotactic bacteria.";
RL   Genome Res. 19:1801-1808(2009).
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; AP010904; BAH74419.1; -; Genomic_DNA.
DR   RefSeq; WP_012750490.1; NC_012796.1.
DR   AlphaFoldDB; C4XKM8; -.
DR   SMR; C4XKM8; -.
DR   STRING; 573370.DMR_09290; -.
DR   EnsemblBacteria; BAH74419; BAH74419; DMR_09290.
DR   KEGG; dma:DMR_09290; -.
DR   eggNOG; COG2060; Bacteria.
DR   HOGENOM; CLU_018614_3_0_7; -.
DR   OMA; RQGWAIL; -.
DR   Proteomes; UP000009071; Chromosome.
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..582
FT                   /note="Potassium-transporting ATPase potassium-binding
FT                   subunit"
FT                   /id="PRO_1000204783"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        304..324
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        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT   TRANSMEM        546..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ   SEQUENCE   582 AA;  61223 MW;  96A7673879537F1F CRC64;
     MNPINLVQLL FFLSVLLVLS WPLGLYAARV YQGQPCVMDK ILGPLERLLY RISGVDASRE
     MDWKIYALVM LGLNAFGMVF VYVLERLQGG LPLNPLHLPG VDPFVAVNTA VSFATNTNWQ
     AYAGESTMSI LTQMLGLAVQ NFLSAATGMA VAVALIRGLA RRETTHLGNF WQDLTRSVLY
     ILLPLSFVLA LLLVWQGVPQ TFTGQVEADW LDPAPHVAES ISPDTPSTDQ PPAKQTIVLG
     PVASQVAIKQ LGTNGGGYFN VNSAHPLENP TPLTNLLEML AILLIPAALC HTFGVMIGDR
     RQGLAILAAM TILFAGFAAL TLAAESVPNP TLSGIGVPAV PSLEGKEVRF GTAGSALWAA
     ATTAASNGSV NAMHDSFSPL GGMWPMLLMQ LGEVVYGGVG SGLYGMLVFA VVTVFVAGLM
     VGRTPEYCGK KIEPFETKMA ALVILIPPFL CLAGTALAAV IGPADAVSNP GPHGFSQMLY
     AFSSMGNNNG SAFAGLTATS PFWTIAGAVA MFVSRYWLIV PVLALAGSLA GKKRLAQGPG
     TLPTHGGIFV ALLIIVVLVV GALTFVPALA LGPIAEQLAL FQ