KDPB2_LISIN
ID KDPB2_LISIN Reviewed; 686 AA.
AC Q926K7;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Potassium-transporting ATPase ATP-binding subunit 2 {ECO:0000255|HAMAP-Rule:MF_00285};
DE EC=7.2.2.6 {ECO:0000255|HAMAP-Rule:MF_00285};
DE AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain 2 {ECO:0000255|HAMAP-Rule:MF_00285};
DE AltName: Full=Potassium-binding and translocating subunit B 2 {ECO:0000255|HAMAP-Rule:MF_00285};
DE AltName: Full=Potassium-translocating ATPase B chain 2 {ECO:0000255|HAMAP-Rule:MF_00285};
GN Name=kdpB2 {ECO:0000255|HAMAP-Rule:MF_00285}; OrderedLocusNames=pli0053;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OG Plasmid pLI100.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16778;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00285};
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC. {ECO:0000255|HAMAP-Rule:MF_00285}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00285};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00285}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IA subfamily. {ECO:0000255|HAMAP-Rule:MF_00285}.
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DR EMBL; AL592102; CAC42051.1; -; Genomic_DNA.
DR RefSeq; WP_011011039.1; NC_003383.1.
DR AlphaFoldDB; Q926K7; -.
DR SMR; Q926K7; -.
DR STRING; 272626.pli0053; -.
DR EnsemblBacteria; CAC42051; CAC42051; CAC42051.
DR KEGG; lin:pli0053; -.
DR eggNOG; COG2216; Bacteria.
DR HOGENOM; CLU_025728_2_0_9; -.
DR OMA; ILWLWFT; -.
DR OrthoDB; 237367at2; -.
DR Proteomes; UP000002513; Plasmid pLI100.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 PANTHER; PTHR43743; PTHR43743; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR TIGRFAMs; TIGR01497; kdpB; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Plasmid; Potassium;
KW Potassium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..686
FT /note="Potassium-transporting ATPase ATP-binding subunit 2"
FT /id="PRO_0000046122"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT ACT_SITE 306
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 376..383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 518
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT BINDING 522
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
SQ SEQUENCE 686 AA; 73593 MW; 1601A6DF0A2534E8 CRC64;
MEKKAKPGFW DKKILGTAVK GAFIKLNPVY MVKNPVMFVV EIGAIISLAL CFFPNLFGGN
NQDMILYNSL VFIILLLTLL FANFSESVAE GRGKAQAASL KQTQQDMQAR LILNGKEKVV
NANTLKKGDI VLVNMGEVIP SDGEIIEGVA SVDESAITGE SAPVLKESGG DFASVTGGTT
VASDYLKIQI TSNPGESFID KMIQLVEGAS RKKTPNEIAL STLLVSLTII FLIVIVSLYP
MAIYTGIKLP VSTLVALTVC LIPTTIGGLL SAIGIAGMDR VTRFNVIALS GKAVEACGDV
DTMILDKTGT ITYGNRMASE FIALDKGNKN YLIHYAILAS IQDNTPEGKS IVTLGKDLLK
EDLDTNDIRE NQFIEFTAQT RMSGVDLADG TRIRKGAYDA IIKYIKNIGG EIPHDLEDKV
NNISKLGGTP LVVCAEEKIY GVIYLKDTIK PGLVERFERL RSIGIKTIMC TGDNPLTAAT
IAHEAGVDSF IAECKPEDKI KVIKDAQSKS KVVAMTGDGT NDAPALAQAD VGIAMNSGTT
AAKEAANMVD LDSDPTKILD VVEIGKQLLI TRGALTTFSI ANDIAKYFAI IPAMFLAIIP
QMQVLNIMHL SSSYSAILSA LIFNAIIIPC LIPLAMKGVK YKLQRSEKML AHNMLVYGVG
GMIVPFIGIK LIDLVIAPLL TMMGLG
