THIS_ECOLI
ID THIS_ECOLI Reviewed; 66 AA.
AC O32583; Q2M8S8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Sulfur carrier protein ThiS;
DE AltName: Full=Thiamine biosynthesis protein ThiS;
GN Name=thiS; Synonyms=thiG1; OrderedLocusNames=b4407, JW3955;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8432721; DOI=10.1128/jb.175.4.982-992.1993;
RA Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P.;
RT "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in
RT Escherichia coli K-12.";
RL J. Bacteriol. 175:982-992(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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].
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 FUNCTION, AMPYLATION AT GLY-66, THIOCARBOXYLATION AT GLY-66, INTERACTION
RP WITH THIF, AND MASS SPECTROMETRY.
RC STRAIN=B/r / ATCC 12407;
RX PubMed=9632726; DOI=10.1074/jbc.273.26.16555;
RA Taylor S.V., Kelleher N.L., Kinsland C., Chiu H.-J., Costello C.A.,
RA Backstrom A.D., McLafferty F.W., Begley T.P.;
RT "Thiamin biosynthesis in Escherichia coli. Identification of ThiS
RT thiocarboxylate as the immediate sulfur donor in the thiazole formation.";
RL J. Biol. Chem. 273:16555-16560(1998).
RN [6]
RP MASS SPECTROMETRY.
RX PubMed=10082377; DOI=10.1002/pro.5560070815;
RA Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J.,
RA Begley T.P., McLafferty F.W.;
RT "Efficient sequence analysis of the six gene products (7-74 kDa) from the
RT Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass
RT spectrometry.";
RL Protein Sci. 7:1796-1801(1998).
RN [7]
RP CROSS-LINKING TO THIF, AND REACTION MECHANISM.
RC STRAIN=K12;
RX PubMed=11438688; DOI=10.1073/pnas.141226698;
RA Xi J., Ge Y., Kinsland C., McLafferty F.W., Begley T.P.;
RT "Biosynthesis of the thiazole moiety of thiamin in Escherichia coli:
RT identification of an acyldisulfide-linked protein--protein conjugate that
RT is functionally analogous to the ubiquitin/E1 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8513-8518(2001).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=11135670; DOI=10.1038/83041;
RA Wang C., Xi J., Begley T.P., Nicholson L.K.;
RT "Solution structure of ThiS and implications for the evolutionary roots of
RT ubiquitin.";
RL Nat. Struct. Biol. 8:47-51(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH THIF, AND REACTION
RP MECHANISM.
RX PubMed=16388576; DOI=10.1021/bi051502y;
RA Lehmann C., Begley T.P., Ealick S.E.;
RT "Structure of the Escherichia coli ThiS-ThiF complex, a key component of
RT the sulfur transfer system in thiamin biosynthesis.";
RL Biochemistry 45:11-19(2006).
CC -!- FUNCTION: Is the sulfur donor in the synthesis of the thiazole
CC phosphate moiety of thiamine phosphate. {ECO:0000269|PubMed:9632726}.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC adenylated (-COAMP) by ThiF, then thiocarboxylated (-COSH) by ThiI.
CC {ECO:0000269|PubMed:9632726}.
CC -!- MASS SPECTROMETRY: Mass=7310.75; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9632726};
CC -!- MASS SPECTROMETRY: Mass=7310.74; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10082377};
CC -!- SIMILARITY: Belongs to the sulfur carrier protein ThiS family.
CC {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; M88701; AAB95620.1; -; Genomic_DNA.
DR EMBL; U00006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAT48237.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77328.1; -; Genomic_DNA.
DR PIR; S77700; S77700.
DR RefSeq; WP_001166226.1; NZ_SSZK01000047.1.
DR RefSeq; YP_026279.1; NC_000913.3.
DR PDB; 1F0Z; NMR; -; A=1-66.
DR PDB; 1ZUD; X-ray; 1.98 A; 2/4=1-66.
DR PDBsum; 1F0Z; -.
DR PDBsum; 1ZUD; -.
DR AlphaFoldDB; O32583; -.
DR BMRB; O32583; -.
DR SMR; O32583; -.
DR BioGRID; 4261404; 4.
DR ComplexPortal; CPX-2134; ThiF-ThiS complex.
DR IntAct; O32583; 1.
DR STRING; 511145.b4407; -.
DR PaxDb; O32583; -.
DR EnsemblBacteria; AAT48237; AAT48237; b4407.
DR EnsemblBacteria; BAE77328; BAE77328; BAE77328.
DR GeneID; 2847702; -.
DR KEGG; ecj:JW3955; -.
DR KEGG; eco:b4407; -.
DR PATRIC; fig|1411691.4.peg.2720; -.
DR EchoBASE; EB4108; -.
DR eggNOG; COG2104; Bacteria.
DR HOGENOM; CLU_174611_2_1_6; -.
DR InParanoid; O32583; -.
DR OMA; MRILFND; -.
DR PhylomeDB; O32583; -.
DR BioCyc; EcoCyc:THIS-MON; -.
DR BioCyc; MetaCyc:THIS-MON; -.
DR UniPathway; UPA00060; -.
DR EvolutionaryTrace; O32583; -.
DR PRO; PR:O32583; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1902503; C:adenylyltransferase complex; IPI:ComplexPortal.
DR GO; GO:1990228; C:sulfurtransferase complex; IC:ComplexPortal.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0097163; F:sulfur carrier activity; IDA:EcoCyc.
DR GO; GO:0018117; P:protein adenylylation; IDA:ComplexPortal.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0052837; P:thiazole biosynthetic process; IDA:EcoCyc.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR010035; Thi_S.
DR InterPro; IPR003749; ThiS/MoaD-like.
DR PANTHER; PTHR34472; PTHR34472; 1.
DR Pfam; PF02597; ThiS; 1.
DR SUPFAM; SSF54285; SSF54285; 1.
DR TIGRFAMs; TIGR01683; thiS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Thiamine biosynthesis; Thioester bond.
FT CHAIN 1..66
FT /note="Sulfur carrier protein ThiS"
FT /id="PRO_0000072518"
FT MOD_RES 66
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000269|PubMed:9632726"
FT MOD_RES 66
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000269|PubMed:9632726"
FT CROSSLNK 66
FT /note="Glycyl cysteine dithioester (Gly-Cys) (interchain
FT with C-184 in ThiF); alternate"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1ZUD"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1F0Z"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1ZUD"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1ZUD"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1ZUD"
SQ SEQUENCE 66 AA; 7311 MW; 9AB3C87835758B40 CRC64;
MQILFNDQAM QCAAGQTVHE LLEQLDQRQA GAALAINQQI VPREQWAQHI VQDGDQILLF
QVIAGG
