PBP_BRUA2
ID PBP_BRUA2 Reviewed; 350 AA.
AC Q2YKI6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Purine-binding protein BAB2_0673;
DE Flags: Precursor;
GN OrderedLocusNames=BAB2_0673;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
CC -!- FUNCTION: Binds adenine and probably also other purines, such as
CC guanine. May play a role in adenine and guanine uptake. May be part of
CC an ABC-type uptake system for adenine and similar ligands (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BMP lipoprotein family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Cys that is essential for lipidation.
CC {ECO:0000305}.
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DR EMBL; AM040265; CAJ12839.1; -; Genomic_DNA.
DR PDB; 3S99; X-ray; 2.05 A; A=17-350.
DR PDBsum; 3S99; -.
DR AlphaFoldDB; Q2YKI6; -.
DR SMR; Q2YKI6; -.
DR STRING; 359391.BAB2_0673; -.
DR EnsemblBacteria; CAJ12839; CAJ12839; BAB2_0673.
DR KEGG; bmf:BAB2_0673; -.
DR PATRIC; fig|359391.11.peg.2857; -.
DR HOGENOM; CLU_038813_2_0_5; -.
DR OMA; PYTNMPD; -.
DR Proteomes; UP000002719; Chromosome II.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR InterPro; IPR003760; PnrA-like.
DR Pfam; PF02608; Bmp; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..350
FT /note="Purine-binding protein BAB2_0673"
FT /id="PRO_0000412071"
FT BINDING 36
FT /ligand="adenine"
FT /ligand_id="ChEBI:CHEBI:16708"
FT BINDING 185
FT /ligand="adenine"
FT /ligand_id="ChEBI:CHEBI:16708"
FT BINDING 211
FT /ligand="adenine"
FT /ligand_id="ChEBI:CHEBI:16708"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 36..51
FT /evidence="ECO:0007829|PDB:3S99"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3S99"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 250..261
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:3S99"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 289..303
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:3S99"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:3S99"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:3S99"
SQ SEQUENCE 350 AA; 38404 MW; 4ED7EE367362ADC7 CRC64;
MVIATVAGFM LGGAAHAEEK LKVGFIYIGP PGDFGWTYQH DQARKELVEA LGDKVETTFL
ENVAEGADAE RSIKRIARAG NKLIFTTSFG YMDPTVKVAK KFPDVKFEHA TGYKTADNMS
AYNARFYEGR YVQGVIAAKM SKKGIAGYIG SVPVPEVVQG INSFMLGAQS VNPDFRVKVI
WVNSWFDPGK EADAAKALID QGVDIITQHT DSTAAIQVAH DRGIKAFGQA SDMIKFAPDT
QLTAVVDEWG PYYIDRAKAV LDGTWKSQNI WWGMKEGLVK MAPFTNMPDD VKKLAEETEA
RIKSGELNPF TGPIKKQDGS EWLKAGEKAD DQTLLGMNFY VAGVDDKLPQ