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Database: UniProt
Entry: A0A0R1MLH5_9LACO
LinkDB: A0A0R1MLH5_9LACO
Original site: A0A0R1MLH5_9LACO 
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
//
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