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Database: UniProt
Entry: Q8U9D9
LinkDB: Q8U9D9
Original site: Q8U9D9 
ID   KDPB_AGRFC              Reviewed;         694 AA.
AC   Q8U9D9;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   20-JAN-2016, entry version 107.
DE   RecName: Full=Potassium-transporting ATPase ATP-binding subunit {ECO:0000255|HAMAP-Rule:MF_00285};
DE            EC=3.6.3.12 {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=Atu3789; ORFNames=AGR_L_2090;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium
OS   tumefaciens (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P.,
RA   Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L.,
RA   Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr.,
RA   Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C.,
RA   Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A.,
RA   Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D.,
RA   Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M.,
RA   Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M.,
RA   Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V.,
RA   Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M.,
RA   Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L.,
RA   Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F.,
RA   Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B.,
RA   Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G.,
RA   Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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: ATP + H(2)O + K(+)(Out) = ADP + phosphate +
CC       K(+)(In). {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)
CC       (TC 3.A.3) family. Type IA subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00285}.
DR   EMBL; AE007870; AAK89619.2; -; Genomic_DNA.
DR   PIR; A98262; A98262.
DR   PIR; AI3022; AI3022.
DR   RefSeq; NP_356834.2; NC_003063.2.
DR   RefSeq; WP_010973322.1; NC_003063.2.
DR   ProteinModelPortal; Q8U9D9; -.
DR   STRING; 176299.Atu3789; -.
DR   EnsemblBacteria; AAK89619; AAK89619; Atu3789.
DR   GeneID; 1135663; -.
DR   KEGG; atu:Atu3789; -.
DR   PATRIC; 20817036; VBIAgrTum91616_3627.
DR   eggNOG; ENOG4105C8X; Bacteria.
DR   eggNOG; COG2216; LUCA.
DR   HOGENOM; HOG000244113; -.
DR   KO; K01547; -.
DR   OrthoDB; EOG6742RM; -.
DR   BioCyc; AGRO:ATU3789-MONOMER; -.
DR   BioCyc; RETL1328306-WGS:GSTH-6124-MONOMER; -.
DR   Proteomes; UP000000813; Chromosome linear.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008556; F:potassium-transporting ATPase activity; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.70.150.10; -; 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_domN.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006391; P-type_ATPase_bsu_IA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SUPFAM; SSF56784; SSF56784; 3.
DR   SUPFAM; SSF81660; SSF81660; 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; Complete proteome;
KW   Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    694       Potassium-transporting ATPase ATP-binding
FT                                subunit.
FT                                /FTId=PRO_0000046108.
FT   TRANSMEM     36     56       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM     62     82       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM    218    238       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM    249    269       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM    600    620       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM    628    648       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   TRANSMEM    666    686       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   NP_BIND     376    383       ATP. {ECO:0000255|HAMAP-Rule:MF_00285}.
FT   ACT_SITE    306    306       4-aspartylphosphate intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00285}.
FT   METAL       530    530       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   METAL       534    534       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00285}.
FT   BINDING     343    343       ATP. {ECO:0000255|HAMAP-Rule:MF_00285}.
FT   BINDING     347    347       ATP. {ECO:0000255|HAMAP-Rule:MF_00285}.
FT   BINDING     394    394       ATP. {ECO:0000255|HAMAP-Rule:MF_00285}.
SQ   SEQUENCE   694 AA;  72964 MW;  AD65EC38E6162BE0 CRC64;
     MSQSKQASIL DSRILVPAIA DAFKKLNPRT LARNPVMFVV ATVSVLTTVL FIRDLITGGA
     NLAFSFQINL WLWFTVLFAN FAEAVAEGRG KAQADSLRKT RTETQAKLLN SDDRSQYKMV
     AGDSLKVNDV VLVEAGDIIP SDGEVIEGVA SVNEAAITGE SAPVIRESGG DRSAVTGGTQ
     VLSDWIRVRI TAAAGSTFLD RMISLVEGAE RQKTPNEIAL NILLAGMTLI FVLATATIPS
     FAAYAGGSIP IIVLVALFVT LIPTTIGALL SAIGIAGMDR LVRFNVLAMS GRAVEAAGDV
     DTLLLDKTGT ITLGNRQATD LRPIPGVSEQ ELADAAQLAS LADETPEGRS IVVLAKEKYG
     IRARDMQKLH ATFVPFTAQT RMSGVDFEGA SIRKGAVDAV LAYVDGGALQ HGNAALALKT
     ETDATRAIRA IAEDIAKAGG TPLAVVRDGK LLGVVQLKDI VKGGIRERFA ELRRMGIRTV
     MITGDNPMTA AAIAAEAGVD DFLAQATPEN KLELIREEQA KGKLVAMCGD GTNDAPALAQ
     ADVGVAMNTG TVAAREAGNM VDLDSDPTKL IEIVEIGKQL LMTRGALTTF SIANDIAKYF
     AIIPAMFLAL YPQLGVLNVM GLSTPQSAIL SAIIFNALII IALIPLSLKG VKYRPIGAGA
     LLSRNLVIYG LGGIIVPFIG IKLIDLAVTA LGLA
//
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