ID   THIB_BRUAB              Reviewed;         334 AA.
AC   Q57BC4;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Thiamine-binding periplasmic protein;
DE   Flags: Precursor;
GN   Name=thiB; OrderedLocusNames=BruAb1_1742;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
CC   -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in
CC       thiamine import. {ECO:0000250|UniProtKB:P31550}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ThiQ),
CC       two transmembrane proteins (ThiP) and a solute-binding protein (ThiB).
CC       {ECO:0000250|UniProtKB:Q7CR85}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P31550}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE017223; AAX75060.1; -; Genomic_DNA.
DR   RefSeq; WP_002964841.1; NC_006932.1.
DR   AlphaFoldDB; Q57BC4; -.
DR   SMR; Q57BC4; -.
DR   EnsemblBacteria; AAX75060; AAX75060; BruAb1_1742.
DR   GeneID; 3788281; -.
DR   KEGG; bmb:BruAb1_1742; -.
DR   HOGENOM; CLU_026974_6_0_5; -.
DR   OMA; PTTNWMY; -.
DR   Proteomes; UP000000540; Chromosome I.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0030975; F:thiamine binding; IEA:InterPro.
DR   GO; GO:0015888; P:thiamine transport; IEA:InterPro.
DR   CDD; cd13545; PBP2_TbpA; 1.
DR   InterPro; IPR006059; SBP.
DR   InterPro; IPR005967; ThiB.
DR   InterPro; IPR005948; ThiB-like.
DR   Pfam; PF01547; SBP_bac_1; 1.
DR   TIGRFAMs; TIGR01254; sfuA; 1.
DR   TIGRFAMs; TIGR01276; thiB; 1.
PE   3: Inferred from homology;
KW   Periplasm; Signal; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..334
FT                   /note="Thiamine-binding periplasmic protein"
FT                   /id="PRO_0000282911"
FT   BINDING         64..65
FT                   /ligand="thiamine"
FT                   /ligand_id="ChEBI:CHEBI:18385"
FT                   /evidence="ECO:0000250|UniProtKB:P31550"
FT   BINDING         166..167
FT                   /ligand="thiamine"
FT                   /ligand_id="ChEBI:CHEBI:18385"
FT                   /evidence="ECO:0000250|UniProtKB:P31550"
FT   BINDING         202
FT                   /ligand="thiamine"
FT                   /ligand_id="ChEBI:CHEBI:18385"
FT                   /evidence="ECO:0000250|UniProtKB:P31550"
FT   BINDING         220..223
FT                   /ligand="thiamine"
FT                   /ligand_id="ChEBI:CHEBI:18385"
FT                   /evidence="ECO:0000250|UniProtKB:P31550"
SQ   SEQUENCE   334 AA;  36752 MW;  C8257889CA07F8D3 CRC64;
     MRLLSLLTFS LFAVIGLAPA AQAKDKLTIY TYDSFVSEWG PGPKVKENFE KECDCEVNFV
     ASADGVALLN RLKLEGSKTA ADIVLGLDTN LTTEARASGF FAPSGIDQTN VKVPGNFKDD
     IFVPYDYGYF AVVYDSEKLP NPPKSLKELV EGDPAQKIVL QDPRTATPGL GMLLWMKSVY
     GDEAGAAWQK LQKRVLTVTP GWSEAYGLFT KGEAPMVLSY TTSPAYHMVV EKTDRYKALA
     YPEGNYLQIE LAAQTTTGAK NPLAKKFLAF MTGPGFQDLI PETNWMFPAG KTSKPLPAAF
     DALPKPEKTL LIPPYEVAKN RRLWVNEWLA ATSR