ID A0A0R1MLH5_9LACO Unreviewed; 691 AA.
AC A0A0R1MLH5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
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 ORFNames=FD09_GL001535 {ECO:0000313|EMBL:KRL08767.1};
OS Schleiferilactobacillus perolens DSM 12744.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1423792 {ECO:0000313|EMBL:KRL08767.1, ECO:0000313|Proteomes:UP000051330};
RN [1] {ECO:0000313|EMBL:KRL08767.1, ECO:0000313|Proteomes:UP000051330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12744 {ECO:0000313|EMBL:KRL08767.1,
RC ECO:0000313|Proteomes:UP000051330};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRL08767.1}.
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DR EMBL; AZEC01000020; KRL08767.1; -; Genomic_DNA.
DR RefSeq; WP_057822353.1; NZ_AZEC01000020.1.
DR AlphaFoldDB; A0A0R1MLH5; -.
DR STRING; 1423792.FD09_GL001535; -.
DR PATRIC; fig|1423792.3.peg.1552; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000051330; 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 CDD; cd02078; P-type_ATPase_K; 1.
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};
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};
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 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 61..83
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 221..242
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 262..285
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT TRANSMEM 583..604
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..689
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT ACT_SITE 315
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 385..392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00285"
FT BINDING 403
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 691 AA; 73867 MW; 738C44E7E313EBB1 CRC64;
MAQKEASKKE KLLTGANMWS AVRKLNFNDE RNNPVMFLVY ISAAMTTLLF VLSLFGISDH
IVTSGFIITV AIILWITCWF SNLAEATAEG RGKAQAATLK ASRKDVTAHK LADPDQPEQY
TDVAGPTLNK GDYFLVKANE QIPADGEVVG GAASVDESAI TGESAPVIRE AGGDRSAVTG
GTTVLSDTLV VKVTQEKGHS FMDKMIGMVE GANRQKTPNE IALEILLVAL SIIFVLVTAS
LFTYSKFSAQ LMGQHNPISI VWLIALFVCL APTTIGALLS AIGIAGMSRL NAANVLAMSG
RAIEAAGDVD VLLLDKTGTI TFGNRRASEF IPVAGHTAEE VADAAQLASL ADETPEGRSI
VVLAKKQFNI RGREVGHHQY HFVPFTAQTK MSGVDYQGIE IRKGAAENIQ NYVEQHDHVY
SDECKNAVEK IARQGGTPLV VTKDYNVLGV IALKDIIKPG VKEKFADLRK MGIQTIMITG
DNPVTAAAIA AEAGVDDFLS QATPESKMET IHQYQAKGHL VAMTGDGTND APALAQADVA
VAMNSGTQAA KEAGNMVDLD SSPTKLIDIV RIGKQLLMTR GSLTTFSIAN DISKYFAIIP
AIFMNLYPPL RVLNIMGLSS STSAILSALI FNALIIVALI PLALNGVKYR EIPAAQLLKH
NLWLYGVGGL IVPFIGIKLI DLIITPLLAL L
//