ID A0A2A2F925_9GAMM Unreviewed; 673 AA.
AC A0A2A2F925;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Potassium-transporting ATPase ATP-binding subunit {ECO:0000256|HAMAP-Rule:MF_00285};
DE EC=7.2.2.6 {ECO:0000256|HAMAP-Rule:MF_00285};
DE AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain {ECO:0000256|HAMAP-Rule:MF_00285};
DE AltName: Full=Potassium-binding and translocating subunit B {ECO:0000256|HAMAP-Rule:MF_00285};
DE AltName: Full=Potassium-translocating ATPase B chain {ECO:0000256|HAMAP-Rule:MF_00285};
GN Name=kdpB {ECO:0000256|HAMAP-Rule:MF_00285,
GN ECO:0000313|EMBL:PAU82021.1};
GN ORFNames=CK501_02400 {ECO:0000313|EMBL:PAU82021.1};
OS Halovibrio salipaludis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halovibrio.
OX NCBI_TaxID=2032626 {ECO:0000313|EMBL:PAU82021.1, ECO:0000313|Proteomes:UP000218896};
RN [1] {ECO:0000313|EMBL:PAU82021.1, ECO:0000313|Proteomes:UP000218896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL5-2 {ECO:0000313|EMBL:PAU82021.1,
RC ECO:0000313|Proteomes:UP000218896};
RA Dong X., Zhang G.;
RT "Halovibrio sewagensis sp. nov., isolated from wastewater of high
RT salinity.";
RL Submitted (AUG-2017) 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 is
CC responsible for energy coupling to the transport system and for the
CC release of the potassium ions to the cytoplasm. {ECO:0000256|HAMAP-
CC Rule:MF_00285}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) + phosphate;
CC Xref=Rhea:RHEA:16777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.6; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00285};
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC. {ECO:0000256|HAMAP-Rule:MF_00285}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00285};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00285}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IA subfamily. {ECO:0000256|HAMAP-Rule:MF_00285}.
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:PAU82021.1}.
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DR EMBL; NSKD01000001; PAU82021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2F925; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000218896; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR HAMAP; MF_00285; KdpB; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006391; P-type_ATPase_bsu_IA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01497; kdpB; 1.
DR PANTHER; PTHR43743; POTASSIUM-TRANSPORTING ATPASE ATP-BINDING SUBUNIT; 1.
DR PANTHER; PTHR43743:SF1; POTASSIUM-TRANSPORTING ATPASE ATP-BINDING SUBUNIT; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00285};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00285};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00285};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00285};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00285};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00285};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00285};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00285};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00285};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538, ECO:0000256|HAMAP-
KW Rule:MF_00285}; Reference proteome {ECO:0000313|Proteomes:UP000218896};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_00285};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00285};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00285};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00285}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 213..234
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 246..268
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 580..601
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 607..630
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT ACT_SITE 301
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 368..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
SQ SEQUENCE 673 AA; 70320 MW; 01C970A801B9E4A5 CRC64;
MSRKPDTTMQ SIKMGEILIQ SLSRLSPRSL ARNPVMFVVA VGTVVTALLA GAHMTQGVPF
GMDLAIAGIL LVTVLFANGA ESIAEARGKA QAGALRATRE NLQARKVTDK GEESIAAGDL
RKGDRVRVRP DELIPGDGEI VEGASTINES AVTGESAPVL REAGTDNSGV SAGTKVLSDE
IVVEITVDPG NSLLDRMIAL VEGAKRQKTP NELALSVLLA AMTLVFLIVV VSLVPTSGFV
GIDPSYSVLV ALLVCLIPTT IGGLLPAIGI AGMDRAMRAN VIAKSGKAVE VAGSVDTLLL
DKTGTITLGD RRATAFETTP GVAAEELRDA ALLTSLADPT PEGKSVVTLA GDQGSTAKAG
EDVRFVEFSA TTRMSGIDFP DGRQLRKGAT DAIRNFVVEK GGHYPDEADR LAERVAQKGA
TPLVVAEGGR VLGVIALSDV IKGGIRERFA RLREMGVKTV MITGDNPTTA AAIAAEAGVD
DFLAEATPEQ KLKFIREEQQ QEGRLVAMMG DGTNDAPALA QADLGLAMNS GTQAAREASN
MVDLDSDPGK LIDVVEIGKQ LLITRGSLTT FSLANDVAKY FAILPALFLA STPALGALNI
LDLSSPMNAV LAATVFNALV IPALIPFALR GVRFKPASAE QLLIRNLLIF GLGGLLLPFP
TIKVLDLIIT VFI
//
