THIB_BRUME
ID THIB_BRUME Reviewed; 334 AA.
AC Q8YJ02;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Thiamine-binding periplasmic protein;
DE Flags: Precursor;
GN Name=thiB; OrderedLocusNames=BMEI0285;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL51466.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008917; AAL51466.1; ALT_INIT; Genomic_DNA.
DR PIR; AG3287; AG3287.
DR RefSeq; WP_004684204.1; NZ_GG703781.1.
DR AlphaFoldDB; Q8YJ02; -.
DR SMR; Q8YJ02; -.
DR STRING; 224914.BMEI0285; -.
DR EnsemblBacteria; AAL51466; AAL51466; BMEI0285.
DR GeneID; 29593036; -.
DR KEGG; bme:BMEI0285; -.
DR PATRIC; fig|224914.52.peg.1212; -.
DR eggNOG; COG4143; Bacteria.
DR OMA; PTTNWMY; -.
DR PhylomeDB; Q8YJ02; -.
DR Proteomes; UP000000419; 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_0000282913"
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; 36737 MW; E0AF4211C40716CC CRC64;
MRLLSLLTFS LFAVIGLAPA AQAKDKLTIY TYDSFVSEWG PGPKVKENFE KECDCEVNFV
ASADGVALLN RLKLEGSKTA ADIVLGLDTN LTTEARASGF FAPSGIDQTN VKVPGNFKDD
IFVPYDYGYF AVVYDSEKLP NPPKSLKELV EGDPAQKIVL QDPRTATPGL GMLLWMKSVY
GDEAGAAWQK LQKRVLTVTP GWSEAYGLFT KGEAPMVLSY TTSPAYHMVV EKTNRYKALA
YPEGNYLQIE LAAQTTTGAK NPLAKKFLAF MTGPGFQDVI PETNWMFPAG KTSKPLPAAF
DALPKPEKTL LIPPYEVAKN RRLWVNEWLA ATSR
