(data stored in ACNUC7421 zone)

SWISSPROT: B4STF2_STRM5

ID   B4STF2_STRM5            Unreviewed;       685 AA.
AC   B4STF2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 88.
DE   RecName: Full=Potassium-transporting ATPase ATP-binding subunit {ECO:0000256|HAMAP-Rule:MF_00285};
DE            EC=7.2.2.6 {ECO:0000256|HAMAP-Rule:MF_00285};
DE   AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain {ECO:0000256|HAMAP-Rule:MF_00285};
DE   AltName: Full=Potassium-binding and translocating subunit B {ECO:0000256|HAMAP-Rule:MF_00285};
DE   AltName: Full=Potassium-translocating ATPase B chain {ECO:0000256|HAMAP-Rule:MF_00285};
GN   Name=kdpB {ECO:0000256|HAMAP-Rule:MF_00285};
GN   OrderedLocusNames=Smal_0290 {ECO:0000313|EMBL:ACF49995.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49995.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49995.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49995.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00285,
CC       ECO:0000256|SAAS:SAAS00987028}.
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:0000256|HAMAP-Rule:MF_00285,
CC         ECO:0000256|SAAS:SAAS01131062};
CC   -!- SUBUNIT: The system is composed of three essential subunits: KdpA,
CC       KdpB and KdpC. {ECO:0000256|HAMAP-Rule:MF_00285,
CC       ECO:0000256|SAAS:SAAS00822521}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00285}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00285}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IA subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00285, ECO:0000256|SAAS:SAAS00822561}.
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DR   EMBL; CP001111; ACF49995.1; -; Genomic_DNA.
DR   RefSeq; WP_012509819.1; NC_011071.1.
DR   STRING; 391008.Smal_0290; -.
DR   EnsemblBacteria; ACF49995; ACF49995; Smal_0290.
DR   KEGG; smt:Smal_0290; -.
DR   eggNOG; ENOG4105C8X; Bacteria.
DR   eggNOG; COG2216; LUCA.
DR   HOGENOM; HOG000244113; -.
DR   KO; K01547; -.
DR   OMA; ILWLWFT; -.
DR   OrthoDB; 237367at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01470-MONOMER; -.
DR   Proteomes; UP000001867; 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   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; 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; B4STF2.
DR   SWISS-2DPAGE; B4STF2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830384};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00285};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822569};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822424};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830374};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830366};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822519};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830373};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00285};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822444};
KW   Potassium transport {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822397};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS01133003};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830386};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00830383};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00285,
KW   ECO:0000256|SAAS:SAAS00822492}.
FT   TRANSMEM     44     61       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM     67     87       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    224    247       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    259    279       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    590    613       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    619    639       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   TRANSMEM    659    683       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   NP_BIND     379    386       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   ACT_SITE    312    312       4-aspartylphosphate intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   METAL       521    521       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   METAL       525    525       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00285}.
FT   BINDING     349    349       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   BINDING     353    353       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
FT   BINDING     398    398       ATP. {ECO:0000256|HAMAP-Rule:MF_00285}.
SQ   SEQUENCE   685 AA;  70792 MW;  2A3401AD1FF22284 CRC64;
     MSTQASSTRS THAPRPALLD GAGLRRALIE AVLKLSPMHL VRSPVMAVVM AGTIVAAIVT
     LTGNAPLGFG LAVTAILLVT VLFGNFAEAV AEARGRGQAA SLRRARQDLV ARRLATPQPG
     AAETQVPAAE LRPGDHVIVS AGELVPADGE IVQGLATINE AAVTGESAPV LREAGTDRSG
     VIGGTKVLSD QIIVRVTAEP GHSFLDRMIA LVEGANRQKT PNEIALTLLL AAMTLTFLVV
     VATLPAIGAS VGVKVDPLLL IALLVCLIPT TIGGLLPAIG IAGMNRALAA NVLAKSGKAV
     EVAGDVDVLL LDKTGTITYG DRQASHFHPL AGIDASQLRE AALLSSLADP TPEGKSIVRL
     AREQGCATAE PDHADYLAFS AQTRMSGVDL EHGRQIRKGA ADAIRAHVQA LGGSVPAELA
     GRVEQVARNG ATPLVVAEGR HVLGVIELSD VVKHGMREKF AQLRAMGIRT VMITGDNPLT
     AAAIAAEAGV DDYIAEARPE DKLARIRQEQ AGGRLVAMVG DGTNDAPALA QADIGLAMNS
     GTQAAKEAGN MVDLDSDPAK LLAVVEVGKQ QLITRGALTT FSLANDVSKY FAILPALFAA
     AVPTMAALNV MQLSSPRNAV LAALIFNALV IPALIPLALR GVRFRPATAT ALLRRNMLVY
     GLGGVLLPFA AIKAIDLLLV LVFGA
//

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