O32583 (THIS_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sulfur carrier protein ThiS

Alternative name(s):
Thiamine biosynthesis protein ThiS

Gene names

Name:	thiS
Synonyms:	thiG1
Ordered Locus Names:	b4407, JW3955

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	66 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate. Ref.5
Pathway	Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Post-translational modification	C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) by ThiF, then thiocarboxylated (-COSH) by ThiI.
Sequence similarities	Belongs to the sulfur carrier protein ThiS family.
Mass spectrometry	Molecular mass is 7310.75 Da from positions 1 - 66. Determined by ESI. Ref.5 Molecular mass is 7310.74 Da from positions 1 - 66. Determined by ESI. Ref.6

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Ligand	Nucleotide-binding
PTM	Thioester bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	thiamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW thiamine diphosphate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 66

66

Sulfur carrier protein ThiS

PRO_0000072518

Amino acid modifications

Modified residue

66

1

1-thioglycine; alternate

Modified residue

66

1

Glycyl adenylate; alternate

Cross-link

66

Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate

Secondary structure

1

.

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66

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Beta strand

8 – 10

3

Helix

18 – 25

8

Beta strand

32 – 36

5

Beta strand

39 – 41

3

Helix

43 – 45

3

Turn

46 – 48

3

Beta strand

56 – 61

6

Sequences

	Sequence		Length	Mass (Da)
	O32583 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 9AB3C87835758B40	FASTA	66	7,311
	10 20 30 40 50 60 MQILFNDQAM QCAAGQTVHE LLEQLDQRQA GAALAINQQI VPREQWAQHI VQDGDQILLF QVIAGG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in Escherichia coli K-12." Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P. J. Bacteriol. 175:982-992(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Thiamin biosynthesis in Escherichia coli. Identification of ThiS thiocarboxylate as the immediate sulfur donor in the thiazole formation." Taylor S.V., Kelleher N.L., Kinsland C., Chiu H.-J., Costello C.A., Backstrom A.D., McLafferty F.W., Begley T.P. J. Biol. Chem. 273:16555-16560(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ACYL ADENYLATION AT GLY-66, THIOCARBOXYLATION AT GLY-66, INTERACTION WITH THIF, MASS SPECTROMETRY. Strain: B/r / ATCC 12407.
[6]	"Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry." Kelleher N.L., Taylor S.V., Grannis D., Kinsland C., Chiu H.-J., Begley T.P., McLafferty F.W. Protein Sci. 7:1796-1801(1998) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY.
[7]	"Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide-linked protein--protein conjugate that is functionally analogous to the ubiquitin/E1 complex." Xi J., Ge Y., Kinsland C., McLafferty F.W., Begley T.P. Proc. Natl. Acad. Sci. U.S.A. 98:8513-8518(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO THIF, REACTION MECHANISM. Strain: K12.
[8]	"Solution structure of ThiS and implications for the evolutionary roots of ubiquitin." Wang C., Xi J., Begley T.P., Nicholson L.K. Nat. Struct. Biol. 8:47-51(2001) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[9]	"Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis." Lehmann C., Begley T.P., Ealick S.E. Biochemistry 45:11-19(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH THIF, REACTION MECHANISM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M88701 Genomic DNA. Translation: AAB95620.1.
U00006 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAT48237.1.
AP009048 Genomic DNA. Translation: BAE77328.1.

PIR

S77700.

RefSeq

YP_026279.1. NC_000913.2.
YP_491469.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F0Z	NMR	-	A	1-66	[»]
1ZUD	X-ray	1.98	2/4	1-66	[»]

ProteinModelPortal

O32583.

SMR

O32583. Positions 1-66.

ModBase

Search...

Protein-protein interaction databases

STRING

511145.b4407.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAT48237; AAT48237; b4407.
BAE77328; BAE77328; BAE77328.

GeneID

12932410.
2847702.

KEGG

ecj:Y75_p3205.
eco:b4407.

PATRIC

32123505. VBIEscCol129921_4105.

Organism-specific databases

EchoBASE

EB4108.

EcoGene

EG14363. thiS.

Phylogenomic databases

eggNOG

COG2104.

HOGENOM

HOG000248060.

KO

K03154.

OMA

CATGQTV.

ProtClustDB

PRK08053.

Enzyme and pathway databases

BioCyc

EcoCyc:THIS-MONOMER.
ECOL316407:JW3955-MONOMER.
MetaCyc:THIS-MONOMER.

UniPathway

UPA00060.

Gene expression databases

Genevestigator

O32583.

Family and domain databases

Gene3D

3.10.20.30. 1 hit.

InterPro

IPR012675. Beta-grasp_dom.
IPR016155. Mopterin_synth/thiamin_S_b.
IPR010035. Thi_S.
IPR003749. ThiS/MoaD.
[Graphical view]

Pfam

PF02597. ThiS. 1 hit.
[Graphical view]

SUPFAM

SSF54285. Mo_synth/thiamin_syn_S_b-grasp. 1 hit.

TIGRFAMs

TIGR01683. thiS. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O32583.

Entry information

Entry name

THIS_ECOLI

Accession

Primary (citable) accession number: O32583
Secondary accession number(s): Q2M8S8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program