THIB_ECOLI
ID THIB_ECOLI Reviewed; 327 AA.
AC P31550; P75637;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Thiamine-binding periplasmic protein;
DE Flags: Precursor;
GN Name=thiB; Synonyms=tbpA, yabL; OrderedLocusNames=b0068, JW0067;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RA Hollenbach A.D., Dickson K.A., Washabaugh M.W.;
RT "E. coli periplasmic thiamin binding protein: cloning, overexpression,
RT purification, and characterization.";
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 1-12.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 19-47, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12182833; DOI=10.1016/s1046-5928(02)00031-1;
RA Hollenbach A.D., Dickson K.A., Washabaugh M.W.;
RT "Overexpression, purification, and characterization of the periplasmic
RT space thiamin-binding protein of the thiamin traffic ATPase in Escherichia
RT coli.";
RL Protein Expr. Purif. 25:508-518(2002).
RN [6]
RP FUNCTION IN THIAMINE TRANSPORT, AND ACTIVITY REGULATION.
RC STRAIN=K12 / KG33;
RX PubMed=12175925; DOI=10.1016/s0005-2736(02)00477-7;
RA Hollenbach A.D., Dickson K.A., Washabaugh M.W.;
RT "Thiamine transport in Escherichia coli: the mechanism of inhibition by the
RT sulfhydryl-specific modifier N-ethylmaleimide.";
RL Biochim. Biophys. Acta 1564:421-428(2002).
RN [7] {ECO:0007744|PDB:2QRY}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 19-327 IN COMPLEX WITH THIAMINE
RP MONOPHOSPHATE.
RX PubMed=18177053; DOI=10.1021/bi7018282;
RA Soriano E.V., Rajashankar K.R., Hanes J.W., Bale S., Begley T.P.,
RA Ealick S.E.;
RT "Structural similarities between thiamin-binding protein and thiaminase-I
RT suggest a common ancestor.";
RL Biochemistry 47:1346-1357(2008).
CC -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in
CC thiamine import (PubMed:12175925). Binds thiamine, thiamine phosphate
CC and thiamine diphosphate with high affinity (PubMed:12182833,
CC PubMed:18177053). {ECO:0000269|PubMed:12175925,
CC ECO:0000269|PubMed:12182833, ECO:0000269|PubMed:18177053}.
CC -!- ACTIVITY REGULATION: Transport is inhibited by the sulfhydryl-specific
CC modifier N-ethylmaleimide. {ECO:0000269|PubMed:12175925}.
CC -!- SUBUNIT: Monomer in solution (PubMed:12182833). The complex is composed
CC of two ATP-binding proteins (ThiQ), two transmembrane proteins (ThiP)
CC and a solute-binding protein (ThiB) (By similarity).
CC {ECO:0000250|UniProtKB:Q7CR85, ECO:0000269|PubMed:12182833}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:12182833}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
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DR EMBL; U09984; AAA18833.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73179.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96637.2; -; Genomic_DNA.
DR PIR; D64728; D64728.
DR RefSeq; NP_414610.1; NC_000913.3.
DR RefSeq; WP_001301364.1; NZ_STEB01000010.1.
DR PDB; 2QRY; X-ray; 2.25 A; A/B/C/D=19-327.
DR PDBsum; 2QRY; -.
DR AlphaFoldDB; P31550; -.
DR SMR; P31550; -.
DR BioGRID; 4261341; 31.
DR ComplexPortal; CPX-4387; Thiamine ABC transporter complex.
DR DIP; DIP-10967N; -.
DR IntAct; P31550; 3.
DR STRING; 511145.b0068; -.
DR BindingDB; P31550; -.
DR TCDB; 3.A.1.19.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P31550; -.
DR PaxDb; P31550; -.
DR PRIDE; P31550; -.
DR EnsemblBacteria; AAC73179; AAC73179; b0068.
DR EnsemblBacteria; BAB96637; BAB96637; BAB96637.
DR GeneID; 946306; -.
DR KEGG; ecj:JW0067; -.
DR KEGG; eco:b0068; -.
DR PATRIC; fig|1411691.4.peg.2214; -.
DR EchoBASE; EB1534; -.
DR eggNOG; COG4143; Bacteria.
DR HOGENOM; CLU_026974_6_0_6; -.
DR InParanoid; P31550; -.
DR OMA; PTTNWMY; -.
DR PhylomeDB; P31550; -.
DR BioCyc; EcoCyc:SFUA-MON; -.
DR BioCyc; MetaCyc:SFUA-MON; -.
DR EvolutionaryTrace; P31550; -.
DR PRO; PR:P31550; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0030975; F:thiamine binding; IPI:EcoCyc.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IPI:EcoCyc.
DR GO; GO:0071934; P:thiamine transmembrane transport; IC:ComplexPortal.
DR GO; GO:0015888; P:thiamine transport; IDA:EcoCyc.
DR CDD; cd13545; PBP2_TbpA; 1.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Periplasm; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:12182833"
FT CHAIN 19..327
FT /note="Thiamine-binding periplasmic protein"
FT /id="PRO_0000031705"
FT BINDING 59..60
FT /ligand="thiamine"
FT /ligand_id="ChEBI:CHEBI:18385"
FT /evidence="ECO:0000269|PubMed:18177053,
FT ECO:0007744|PDB:2QRY"
FT BINDING 161..162
FT /ligand="thiamine"
FT /ligand_id="ChEBI:CHEBI:18385"
FT /evidence="ECO:0000269|PubMed:18177053,
FT ECO:0007744|PDB:2QRY"
FT BINDING 197
FT /ligand="thiamine"
FT /ligand_id="ChEBI:CHEBI:18385"
FT /evidence="ECO:0000269|PubMed:18177053,
FT ECO:0007744|PDB:2QRY"
FT BINDING 215..218
FT /ligand="thiamine"
FT /ligand_id="ChEBI:CHEBI:18385"
FT /evidence="ECO:0000269|PubMed:18177053,
FT ECO:0007744|PDB:2QRY"
FT CONFLICT 1..12
FT /note="MLKKCLPLLLLC -> MSAPAVAV (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:2QRY"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:2QRY"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2QRY"
FT STRAND 118..130
FT /evidence="ECO:0007829|PDB:2QRY"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:2QRY"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2QRY"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:2QRY"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:2QRY"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:2QRY"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2QRY"
FT STRAND 240..250
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:2QRY"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:2QRY"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:2QRY"
FT HELIX 307..325
FT /evidence="ECO:0007829|PDB:2QRY"
SQ SEQUENCE 327 AA; 36163 MW; 348A5625FFC94597 CRC64;
MLKKCLPLLL LCTAPVFAKP VLTVYTYDSF AADWGPGPVV KKAFEADCNC ELKLVALEDG
VSLLNRLRME GKNSKADVVL GLDNNLLDAA SKTGLFAKSG VAADAVNVPG GWNNDTFVPF
DYGYFAFVYD KNKLKNPPQS LKELVESDQN WRVIYQDPRT STPGLGLLLW MQKVYGDDAP
QAWQKLAKKT VTVTKGWSEA YGLFLKGESD LVLSYTTSPA YHILEEKKDN YAAANFSEGH
YLQVEVAART AASKQPELAQ KFLQFMVSPA FQNAIPTGNW MYPVANVTLP AGFEKLTKPA
TTLEFTPAEV AAQRQAWISE WQRAVSR
