THIB_BRUA2
ID THIB_BRUA2 Reviewed; 334 AA.
AC Q2YLW8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Thiamine-binding periplasmic protein;
DE Flags: Precursor;
GN Name=thiB; OrderedLocusNames=BAB1_1770;
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: 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; AM040264; CAJ11726.1; -; Genomic_DNA.
DR RefSeq; WP_002964841.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YLW8; -.
DR SMR; Q2YLW8; -.
DR STRING; 359391.BAB1_1770; -.
DR PRIDE; Q2YLW8; -.
DR EnsemblBacteria; CAJ11726; CAJ11726; BAB1_1770.
DR GeneID; 3788281; -.
DR KEGG; bmf:BAB1_1770; -.
DR PATRIC; fig|359391.11.peg.281; -.
DR HOGENOM; CLU_026974_6_0_5; -.
DR OMA; PTTNWMY; -.
DR PhylomeDB; Q2YLW8; -.
DR Proteomes; UP000002719; 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; Reference proteome; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..334
FT /note="Thiamine-binding periplasmic protein"
FT /id="PRO_0000282912"
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
