ID   THIB_BRUSU              Reviewed;         334 AA.
AC   Q8FYV1; G0K797;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Thiamine-binding periplasmic protein;
DE   Flags: Precursor;
GN   Name=thiB; Synonyms=tbpA; OrderedLocusNames=BR1757, BS1330_I1751;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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; AE014291; AAN30656.1; -; Genomic_DNA.
DR   EMBL; CP002997; AEM19073.1; -; Genomic_DNA.
DR   RefSeq; WP_006192518.1; NZ_KN046804.1.
DR   AlphaFoldDB; Q8FYV1; -.
DR   SMR; Q8FYV1; -.
DR   EnsemblBacteria; AEM19073; AEM19073; BS1330_I1751.
DR   GeneID; 45052724; -.
DR   KEGG; bms:BR1757; -.
DR   KEGG; bsi:BS1330_I1751; -.
DR   PATRIC; fig|204722.21.peg.1228; -.
DR   HOGENOM; CLU_026974_6_0_5; -.
DR   OMA; PTTNWMY; -.
DR   PhylomeDB; Q8FYV1; -.
DR   Proteomes; UP000007104; 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_0000282914"
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;  36727 MW;  117BE09E521E1771 CRC64;
     MRLLSLLTFS LFAVIGLAPA AQAKDTLTIY TYDSFVSEWG PGPKVKENFE KECDCEVNFV
     ASADGVALLN RLKLEGSKTA ADIVLGLDTN LTTEARASGF FAPSGIDQTN VKVPGNFKDD
     IFVPYDYGYF AVVYDSEKLP NPPKSLKELV EGDPAQKIVL QDPRTATPGL GMLLWMKSVY
     GDEAGAAWQK LQKRVLTVTP GWSEAYGLFT KGESPMVLSY TTSPAYHMVV EKTDRYKALA
     YPEGNYLQIE LAAQTTTGAK NPLAKKFLAF MTGPGFQDVI PETNWMFPAG KTSKPLPAAF
     DALPKPEKTL LIPPYEVAKN RRLWVNEWLA ATSR