(data stored in ACNUC7421 zone)

SWISSPROT: KDPB_ECO27

ID   KDPB_ECO27              Reviewed;         682 AA.
AC   B7UKX6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
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=E2348C_0586;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Part of the high-affinity ATP-driven potassium transport
CC       (or Kdp) system, which catalyzes the hydrolysis of ATP coupled
CC       with the electrogenic transport of potassium into the cytoplasm.
CC       This subunit is responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_00285}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) +
CC         phosphate; Xref=Rhea:RHEA:16777, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00285};
CC   -!- SUBUNIT: The system is composed of three essential subunits: KdpA,
CC       KdpB 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
CC       3.A.3) family. Type IA subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00285}.
DR   EMBL; FM180568; CAS08134.1; -; Genomic_DNA.
DR   RefSeq; WP_000087998.1; NC_011601.1.
DR   SMR; B7UKX6; -.
DR   EnsemblBacteria; CAS08134; CAS08134; E2348C_0586.
DR   KEGG; ecg:E2348C_0586; -.
DR   KO; K01547; -.
DR   OMA; ILWLWFT; -.
DR   BioCyc; ECOL574521:E2348C_RS03110-MONOMER; -.
DR   Proteomes; UP000008205; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008556; F:potassium-transporting ATPase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02078; P-type_ATPase_K; 1.
DR   Gene3D; 3.40.1110.10; -; 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; IPR006391; P-type_ATPase_bsu_IA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   PANTHER; PTHR43743; PTHR43743; 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;
DR   PRODOM; B7UKX6.
DR   SWISS-2DPAGE; B7UKX6.
KW   ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Potassium; Potassium transport; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    682       Potassium-transporting ATPase ATP-binding
FT                                subunit.
FT                                /FTId=PRO_1000132604.
FT   TRANSMEM     34     54       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM     62     82       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM    219    239       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM    254    274       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM    588    608       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM    616    636       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM    656    676       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   NP_BIND     377    384       ATP. {ECO:0000255|HAMAP-Rule:MF_00285}.
FT   ACT_SITE    307    307       4-aspartylphosphate intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00285}.
FT   METAL       518    518       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   METAL       522    522       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   BINDING     344    344       ATP. {ECO:0000255|HAMAP-Rule:MF_00285}.
FT   BINDING     348    348       ATP. {ECO:0000255|HAMAP-Rule:MF_00285}.
FT   BINDING     395    395       ATP. {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
//

If you have problems or comments...

PBIL Back to PBIL home page