位置:首页 > 蛋白库 > KDPB_ECOL6
KDPB_ECOL6
ID   KDPB_ECOL6              Reviewed;         682 AA.
AC   Q8FJV4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
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}; OrderedLocusNames=c0782;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00285}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       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; AE014075; AAN79255.1; -; Genomic_DNA.
DR   RefSeq; WP_000087998.1; NC_004431.1.
DR   AlphaFoldDB; Q8FJV4; -.
DR   SMR; Q8FJV4; -.
DR   STRING; 199310.c0782; -.
DR   EnsemblBacteria; AAN79255; AAN79255; c0782.
DR   KEGG; ecc:c0782; -.
DR   eggNOG; COG2216; Bacteria.
DR   HOGENOM; CLU_025728_2_0_6; -.
DR   OMA; ILWLWFT; -.
DR   BioCyc; ECOL199310:C0782-MON; -.
DR   Proteomes; UP000001410; 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; SSF81660; SSF81660; 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 inner membrane; Cell membrane; Ion transport; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW   Potassium transport; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..682
FT                   /note="Potassium-transporting ATPase ATP-binding subunit"
FT                   /id="PRO_0000046117"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        254..274
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        307
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         377..384
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   682 AA;  72220 MW;  37C3E200FDB81317 CRC64;
     MSRKQLALFE PTLVVQALKE AVKKLNPQAQ WRNPVMFIVW IGSLLTTCIS IAMASGVMPG
     NALFSAAISG WLWVTVLFAN FAEALAEGRS KAQANSLKGV KKTAFARKLR EPKYGAAADK
     VPADQLRKGD IVLVEAGDII PCDGEVIEGG ASVDESAITG ESAPVIRESG GDFASVTGGT
     RILSDWLVIE CSVNPGETFL DRMIAMVEGA QRRKTPNEIA LTILLIALTI VFLLATATLW
     PFSAWGGNAV SVTVLVALLV CLIPTTIGGL LSAIGVAGMS RMLGANVIAT SGRAVEAAGD
     VDVLLLDKTG TITLGNRQAS EFIPAQGVEE KALADAAQLA SLADETPEGR SIVILAKQRF
     NLRERDVQSL HATFVPFTAQ SRMSGINIDN RMIRKGSVDA IRRHVEANGG HFPADVDQKV
     DQVARQGATP LVVVEGSRVL GVIALKDIVK GGIKERFAQL RKMGIKTVMI TGDNRLTAAA
     IAAEAGVDDF LAEATPEAKL ALIRQYQAEG RLVAMTGDGT NDAPALAQAD VAVAMNSGTQ
     AAKEAGNMVD LDSNPTKLIE VVHIGKQMLM TRGSLTTFSI ANDVAKYFAI IPAAFAATYP
     QLNALNIMRL HSPDSAILSA VIFNALIIVF LIPLALKGVS YKPLTASAML RRNLWIYGLG
     GLLVPFIGIK VIDLLLTVCG LV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024