位置:首页 > 蛋白库 > KDPB_BACC7
KDPB_BACC7
ID   KDPB_BACC7              Reviewed;         697 AA.
AC   B7HWG1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Potassium-transporting ATPase ATP-binding subunit {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 {ECO:0000255|HAMAP-Rule:MF_00285};
DE   AltName: Full=Potassium-binding and translocating subunit B {ECO:0000255|HAMAP-Rule:MF_00285};
DE   AltName: Full=Potassium-translocating ATPase B chain {ECO:0000255|HAMAP-Rule:MF_00285};
GN   Name=kdpB {ECO:0000255|HAMAP-Rule:MF_00285};
GN   OrderedLocusNames=BCAH187_A0895;
OS   Bacillus cereus (strain AH187).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH187;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA   Okstad O.A., Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH187.";
RL   Submitted (OCT-2008) 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: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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001177; ACJ78940.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7HWG1; -.
DR   SMR; B7HWG1; -.
DR   EnsemblBacteria; ACJ78940; ACJ78940; BCAH187_A0895.
DR   KEGG; bcr:BCAH187_A0895; -.
DR   HOGENOM; CLU_025728_2_0_9; -.
DR   OMA; ILWLWFT; -.
DR   Proteomes; UP000002214; Chromosome.
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   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; Potassium;
KW   Potassium transport; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..697
FT                   /note="Potassium-transporting ATPase ATP-binding subunit"
FT                   /id="PRO_1000119407"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        605..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        633..653
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        677..697
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   ACT_SITE        324
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         361
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         365
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         393..400
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         412
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         535
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
SQ   SEQUENCE   697 AA;  74683 MW;  A5EA27019A43ED71 CRC64;
     MMRPVVVKEK RVNESQIHVV EEEVRQAKTM DRDIVTHAMK QSFAKLNPKV MIKNPIMFVV
     EIGFIITFIL SFLPSHSSSV PGWFNITVSF ILLFTVLFAN FAEALAEGRG KAQADSLKHS
     KKDVFANVVK ENGNIVQVSA TDLRKGDVVI VKQGEMIPSD GEVIKGLASV DESAITGESA
     PVIKEAGGDF CSVTGGTMVV SDEITIIITS NPGESFIDKM ISLVEGAARQ KTPNEIALNT
     VLTSLTFIFL IVVVTLPIFT NYLGFQIDTA VLVALLVCLI PTTIGGLLSA IGIAGMDRVT
     KFNVLAMSGK AVEAAGDINT IILDKTGTIT FGNRMAHTLL PVGNETIEQV GKWAAISSVL
     DETPEGRSVI EYVQAKSISY NRELAEQGEF VPFKAETRMS GVDLQDGTKV RKGAVGSVIE
     WVQSQGGTIP KDVNQKADFI SKEGGTPLVV AVNNRIYGLI YLKDTVKPGM RERFEQLRQM
     GIKTVMCTGD NPLTAATIAK EAGVDEFVAE CKPEDKIAVI KAEQDKGKLV AMTGDGTNDA
     PALAQADVGL AMNSGTTAAK EAANMIDLDS NPTKIIEVVG IGKQLLMTRG ALTTFSIAND
     IAKYFAIIPA MFTLAIPQME ALNIMKLTSP LSAILSALLF NAVIIPLLIP LAMKGIAYKP
     MSSNALLGRN LLIYGLGGVI VPFIGIKVID MIVGLFI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024