ID A0A327M6U7_9PROT Unreviewed; 690 AA.
AC A0A327M6U7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:RAI58670.1};
GN ORFNames=DOO78_13375 {ECO:0000313|EMBL:RAI58670.1};
OS Roseicella frigidaeris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Roseicella.
OX NCBI_TaxID=2230885 {ECO:0000313|EMBL:RAI58670.1, ECO:0000313|Proteomes:UP000249065};
RN [1] {ECO:0000313|Proteomes:UP000249065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DB-1506 {ECO:0000313|Proteomes:UP000249065};
RA Khan S.A.;
RL Submitted (JUN-2018) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:RAI58670.1}.
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DR EMBL; QLIX01000008; RAI58670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327M6U7; -.
DR OrthoDB; 391538at2; -.
DR Proteomes; UP000249065; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 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}; Hydrolase {ECO:0000313|EMBL:RAI58670.1};
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:UP000249065};
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 74..98
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 231..254
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 266..289
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 624..644
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 664..687
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT ACT_SITE 319
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 388..395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 526
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
SQ SEQUENCE 690 AA; 71466 MW; B8437E05CC3AB0C4 CRC64;
MPDISDSLQP STAGRSLPGS ALRDRGLLGR AALEALRKLN PHSLIRNPVI FTTEAVSALV
TALAIEAAAT GGAWGFPAAI AVWLWLTVLF ATFAEAVAEG RGRARAESLR RARTETVAKR
LLRPDDRSLW QPRPAAALRP GELVLVEAGD LIPSDGEVVE GVASVNEAAV TGESAPVIRE
SGGDRSAVTG GTLVVSDWLV VRITAAPGST FLDRMIALVE GAARQKTPNE IALDILLAGM
TIIFLIAVVT LVGLASWNGQ PPSVTVLAAL LITLIPTTIG GLLSAIGIAG MDRLLRVNIL
ATSGRAVEAA GDVDVLLLDK TGTITLGNRQ AAGFHPAPGI AERALAEAAA LASLGDETPE
GRSILAFARA QHGIAAPALP PGARIVPFSA ETRLSGLDLP DARYRKGAVD AVARATGAAT
PPALAQAVER IARAGATPLA VAKDGAMLGA IALKDIVKPG IRERFAALRR MGIRTVMVTG
DNRLTAAAIA AEAGVDDVLA EATPEEKLRH IRAAQAEGRL VAMAGDGTND APALAQADVG
LAMQTGTQAA REAGNMVDLD SDPTKLIEVV EIGKQLLITR GALTTFSIAN DVAKYFAILP
AIFAASYPEL QALNLMRLTS PESAILAAVI FNALIIVALV PLALRGVRYR PEGAAALLRR
NLLLYGLGGI LAPFLGIKLI DLALHLLGIV
//
