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KDPB_STAEQ
ID   KDPB_STAEQ              Reviewed;         673 AA.
AC   Q5HK64;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=SERP2486;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53381.1; -; Genomic_DNA.
DR   RefSeq; WP_000852430.1; NC_002976.3.
DR   AlphaFoldDB; Q5HK64; -.
DR   SMR; Q5HK64; -.
DR   STRING; 176279.SERP2486; -.
DR   EnsemblBacteria; AAW53381; AAW53381; SERP2486.
DR   KEGG; ser:SERP2486; -.
DR   eggNOG; COG2216; Bacteria.
DR   HOGENOM; CLU_025728_2_0_9; -.
DR   OMA; TNPGETF; -.
DR   OrthoDB; 237367at2; -.
DR   Proteomes; UP000000531; 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   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; 1.
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; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..673
FT                   /note="Potassium-transporting ATPase ATP-binding subunit"
FT                   /id="PRO_0000046143"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        581..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        609..629
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   TRANSMEM        649..669
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   ACT_SITE        304
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         370..377
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         388
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         511
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
FT   BINDING         515
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00285"
SQ   SEQUENCE   673 AA;  72985 MW;  7DDDD846B0F6B1E6 CRC64;
     MAETTKIFES HLVKQALKDS VLKLYPVYMI KNPIMFVVEV GMLLALGLTI YPDLFHQESV
     SRLYVFSIFI ILLLTLVFAN FSEALAEGRG KAQANALRQT QTEMKARRIK QDGSYEMIDA
     SDLKKGHIVR VATGEQIPND GKVIKGLATV DESAITGESA PVIKESGGDF DNVIGGTSVA
     SDWLEVEITS EPGHSFLDKM IGLVEGATRK KTPNEIALFT LLMTLTIIFL VVILTMYPLA
     KFLNFNLSIA MLIALAVCLI PTTIGGLLSA IGIAGMDRVT QFNILAKSGR SVETCGDVNV
     LILDKTGTIT YGNRMADAFI PVKSSSFERL VKAAYESSIA DDTPEGRSIV KLAYKQHIDL
     PQEVGEYIPF TAETRMSGVK FTTREVYKGA PNSMVKRVKE AGGHIPVDLD ALVKGVSKKG
     GTPLVVLEDN EILGVIYLKD VIKDGLVERF RELREMGIET VMCTGDNELT AATIAKEAGV
     DRFVAECKPE DKINVIREEQ AKGHIVAMTG DGTNDAPALA EANVGLAMNS GTMSAKEAAN
     LIDLDSNPTK LMEVVLIGKQ LLMTRGSLTT FSIANDIAKY FAILPAMFMA AMPAMNHLNI
     MHLHSPESAV LSALIFNALI IVLLIPIAMK GVKFKGASTQ TILMKNMLVY GLGGMIVPFI
     GIKLIDLIIQ LFV
 
 
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