Q81KU0 (THII_BACAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable tRNA sulfurtransferase
EC=2.8.1.4

Alternative name(s):
Sulfur carrier protein ThiS sulfurtransferase
Thiamine biosynthesis protein thiI
tRNA 4-thiouridine synthase

Gene names

Name:	thiI
Ordered Locus Names:	BA_4899, GBAA_4899, BAS4545

Organism

Bacillus anthracis

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by iscS By similarity. HAMAP MF_00021
Catalytic activity	L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide. HAMAP MF_00021 [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + [ThiS]-COSH + AMP. HAMAP MF_00021
Pathway	Cofactor biosynthesis; thiamine diphosphate biosynthesis. HAMAP MF_00021
Subcellular location	Cytoplasm By similarity HAMAP MF_00021.
Sequence similarities	Belongs to the thiI family. Contains 1 THUMP domain.
Sequence caution	The sequence AAT56842.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Thiamine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding RNA-binding tRNA-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	thiamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW transferase activity 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 – 403

403

Probable tRNA sulfurtransferase HAMAP MF_00021

PRO_0000154830

Regions

Domain

60 – 165

106

THUMP

Nucleotide binding

183 – 184

2

ATP HAMAP MF_00021

Nucleotide binding

208 – 209

2

ATP HAMAP MF_00021

Sites

Binding site

265

1

ATP

Binding site

287

1

ATP; via amide nitrogen

Binding site

296

1

ATP

Secondary structure

1

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403

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Helix

18 – 34

17

Turn

35 – 37

3

Beta strand

42 – 45

4

Beta strand

50 – 53

4

Helix

59 – 66

8

Beta strand

72 – 84

13

Helix

85 – 97

13

Beta strand

105 – 112

8

Helix

121 – 133

13

Beta strand

136 – 138

3

Beta strand

143 – 145

3

Beta strand

147 – 154

8

Beta strand

156 – 167

12

Turn

174 – 177

4

Beta strand

179 – 183

5

Beta strand

186 – 188

3

Helix

189 – 199

11

Beta strand

203 – 210

8

Turn

212 – 214

3

Helix

217 – 230

14

Helix

231 – 233

3

Beta strand

237 – 243

7

Helix

245 – 254

10

Helix

257 – 259

3

Helix

260 – 278

19

Beta strand

283 – 285

3

Beta strand

290 – 292

3

Helix

298 – 304

7

Helix

305 – 307

3

Turn

315 – 318

4

Helix

321 – 330

10

Helix

334 – 337

4

Helix

359 – 366

8

Helix

372 – 381

10

Beta strand

383 – 387

5

Sequences

	Sequence		Length	Mass (Da)
	Q81KU0 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: A87E445661268FA6	FASTA	403	45,711
	10 20 30 40 50 60 MTYEYILVRY GEMTTKGKNR SKFVSTLKDN VKFKLKKFPN IKIDATHDRM YIQLNGEDHE 70 80 90 100 110 120 AVSERLKDVF GIHKFNLAMK VPSELEDIKK GALAAFLQVK GDVKTFKITV HRSYKHFPMR 130 140 150 160 170 180 TMELLPEIGG HILENTEDIT VDVHNPDVNV RVEIRSGYSY IMCDERMGAG GLPVGVGGKV 190 200 210 220 230 240 MVLLSGGIDS PVAAYLTMKR GVSVEAVHFH SPPFTSERAK QKVIDLAQEL TKYCKRVTLH 250 260 270 280 290 300 LVPFTEVQKT INKEIPSSYS MTVMRRMMMR ITERIAEERN ALAITTGESL GQVASQTLDS 310 320 330 340 350 360 MHTINEVTNY PVIRPLITMD KLEIIKIAEE IGTYDISIRP YEDCCTVFTP ASPATKPKRE 370 380 390 400 KANRFEAKYD FTPLIDEAVA NKETMVLQTV EVVAEEEKFE ELF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.
[4]	"Crystal structure of Bacillus anthracis ThiI, a tRNA-modifying enzyme containing the predicted RNA-binding THUMP domain." Waterman D.G., Ortiz-Lombardia M., Fogg M.J., Koonin E.V., Antson A.A. J. Mol. Biol. 356:97-110(2006) [PubMed: 16343540] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH AMP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE016879 Genomic DNA. Translation: AAP28584.1.
AE017334 Genomic DNA. Translation: AAT34017.2.
AE017225 Genomic DNA. Translation: AAT56842.1. Different initiation.

RefSeq

NP_847098.1. NC_003997.3.
YP_021542.2. NC_007530.2.
YP_030792.1. NC_005945.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C5S	X-ray	2.50	A	1-403	[»]

ProteinModelPortal

Q81KU0.

SMR

Q81KU0. Positions 3-391.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000012121; EBBACP00000011877; EBBACG00000012113.
EBBACT00000013863; EBBACP00000013484; EBBACG00000013855.
EBBACT00000020175; EBBACP00000019660; EBBACG00000020166.

GeneID

1087273.
2820124.
2850079.

GenomeReviews

Gene locus BA_4899 in contig AE016879_GR.
Gene locus BAS4545 in contig AE017225_GR.
Gene locus GBAA_4899 in contig AE017334_GR.

KEGG

ban:BA_4899.
bar:GBAA_4899.
bat:BAS4545.

TIGR

BA_4899.
GBAA_4899.

Phylogenomic databases

GeneTree

EBGT00050000001800.

HOGENOM

HBG646072.

OMA

DCCTIFV.

ProtClustDB

PRK01565.

Enzyme and pathway databases

BioCyc

BANT260799:BAS4545-MONOMER.
BANT261594:GBAA4899-MONOMER.

Family and domain databases

HAMAP

MF_00021. ThiI.
[Tree]

InterPro

IPR014729. Rossmann-like_a/b/a_fold.
IPR003720. ThiI.
IPR020536. ThiI_C.
IPR004114. THUMP.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

KO

K03151.

Pfam

PF02568. ThiI. 1 hit.
PF02926. THUMP. 1 hit.
[Graphical view]

SMART

SM00981. THUMP. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00342. TIGR00342. 1 hit.

PROSITE

PS51165. THUMP. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

THII_BACAN

Accession

Primary (citable) accession number: Q81KU0
Secondary accession number(s): Q6HS96, Q6KLJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2003
Last sequence update:	June 1, 2003
Last modified:	November 16, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program