THIB_HAEIN
ID THIB_HAEIN Reviewed; 332 AA.
AC P44984;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Thiamine-binding periplasmic protein;
DE Flags: Precursor;
GN Name=thiB; Synonyms=tbpA; OrderedLocusNames=HI_1019;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22678.1; -; Genomic_DNA.
DR PIR; C64164; C64164.
DR RefSeq; NP_439179.1; NC_000907.1.
DR RefSeq; WP_005693356.1; NC_000907.1.
DR AlphaFoldDB; P44984; -.
DR SMR; P44984; -.
DR STRING; 71421.HI_1019; -.
DR EnsemblBacteria; AAC22678; AAC22678; HI_1019.
DR KEGG; hin:HI_1019; -.
DR PATRIC; fig|71421.8.peg.1063; -.
DR eggNOG; COG4143; Bacteria.
DR HOGENOM; CLU_026974_6_0_6; -.
DR OMA; PTTNWMY; -.
DR PhylomeDB; P44984; -.
DR BioCyc; HINF71421:G1GJ1-1059-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0030975; F:thiamine binding; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR GO; GO:0015888; P:thiamine transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR006061; SBP_1_CS.
DR InterPro; IPR005967; ThiB.
DR InterPro; IPR005948; ThiB-like.
DR TIGRFAMs; TIGR01254; sfuA; 1.
DR TIGRFAMs; TIGR01276; thiB; 1.
DR PROSITE; PS01037; SBP_BACTERIAL_1; 1.
PE 3: Inferred from homology;
KW Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..332
FT /note="Thiamine-binding periplasmic protein"
FT /id="PRO_0000031706"
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 332 AA; 37272 MW; 90A27B35D0F9C741 CRC64;
MKLLKLTLIS TALFSTAALA QAQQSVNVYS YDSFTSEWGA GPKVKQDFEK AHPQCAINFT
PFESVGVLLN RVRLEGKKTK ADIVLGLDNF FLEQAEKTGI FAPNNVDLTQ LDLPTKWANK
TFLPFDFGNY AFVYDKTKLQ NPPKSLKELV ERQDLSVIYQ DPRTSSVGRG LLVWMNAVYP
ADKIQSAWKE LDKHTVTVGK GWSDTYGAFL KGEADLVLSY STSPLYHQLF EKKDNYAATD
FAEGHITQVE LAARVANHPN QCADDFMAFL ISPTAQKHIV TANIMLPVIQ GEIEPHFDAL
KVQQKTQTSI NPMVNTEQLK NWISTWQTTL TK
