Y529_BURPS
ID Y529_BURPS Reviewed; 297 AA.
AC Q63XL1;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Nucleotide-binding protein BPSL0529 {ECO:0000255|HAMAP-Rule:MF_00636};
GN OrderedLocusNames=BPSL0529;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- FUNCTION: Displays ATPase and GTPase activities. {ECO:0000255|HAMAP-
CC Rule:MF_00636}.
CC -!- SIMILARITY: Belongs to the RapZ-like family. {ECO:0000255|HAMAP-
CC Rule:MF_00636}.
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DR EMBL; BX571965; CAH34518.1; -; Genomic_DNA.
DR RefSeq; WP_004530937.1; NZ_CP009538.1.
DR RefSeq; YP_107154.1; NC_006350.1.
DR AlphaFoldDB; Q63XL1; -.
DR SMR; Q63XL1; -.
DR STRING; 272560.BPSL0529; -.
DR EnsemblBacteria; CAH34518; CAH34518; BPSL0529.
DR GeneID; 56527225; -.
DR KEGG; bps:BPSL0529; -.
DR PATRIC; fig|272560.51.peg.1119; -.
DR eggNOG; COG1660; Bacteria.
DR OMA; TVMSFGF; -.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00636; RapZ_like; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005337; RapZ-like.
DR PANTHER; PTHR30448; PTHR30448; 1.
DR Pfam; PF03668; ATP_bind_2; 1.
DR PIRSF; PIRSF005052; P-loopkin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..297
FT /note="Nucleotide-binding protein BPSL0529"
FT /id="PRO_0000107695"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
FT BINDING 57..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
SQ SEQUENCE 297 AA; 33195 MW; 5B42CF3973D108B4 CRC64;
MRIVLITGIS GSGKSVALNA LEDAGYYCVD NLPPHVLPEL ARYLAHEGQN RLAVAIDARS
SASLDEMPGL IRALSREHDV RVLFLNASTQ ALIQRFSETR RRHPLSGSPS HDADVGLLVS
LEEAIERERE LVAPLAEFGH QIDTSNLRAN VLRTWVKRFI EQKNDDLVLM FESFGFKRGV
PLDADFMFDV RALPNPYYDH ELRPLTGLDQ PVVAFLDALP VVHQMLDDIE TFLVKWLPHF
REDNRSYLTV AIGCTGGQHR SVFLAETLAA RLSRQASVIV RHRDAPVAVD ASSRLVT
