Reviewed, UniProtKB/Swiss-Prot P00953 (SYW_BACST)

Names and origin

Protein names

Recommended name:
    Tryptophanyl-tRNA synthetase
    EC=6.1.1.2
Alternative name(s):
    Tryptophan--tRNA ligase
      Short name=TrpRS

Gene names

Name:

trpS

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp). HAMAP MF_00140
Subunit structure	Homodimer. HAMAP MF_00140
Subcellular location	Cytoplasm. HAMAP MF_00140
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	tryptophanyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP tryptophan-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 328

328

Tryptophanyl-tRNA synthetase HAMAP MF_00140

PRO_0000136601

Regions

Motif

10 – 18

9

"HIGH" region HAMAP MF_00140

Motif

192 – 196

5

"KMSKS" region HAMAP MF_00140

Sites

Binding site

195

1

ATP By similarity

Secondary structure

1

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328

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

16 – 21

6

Helix

23 – 29

7

Turn

30 – 32

3

Beta strand

33 – 39

7

Helix

41 – 44

4

Helix

51 – 67

17

Turn

72 – 74

3

Beta strand

75 – 79

5

Helix

80 – 82

3

Helix

85 – 96

12

Helix

99 – 103

5

Helix

106 – 112

7

Helix

120 – 123

4

Helix

125 – 134

10

Turn

135 – 137

3

Beta strand

139 – 142

4

Helix

145 – 147

3

Helix

148 – 165

18

Beta strand

173 – 175

3

Beta strand

178 – 182

5

Helix

200 – 202

3

Helix

210 – 219

10

Turn

232 – 234

3

Helix

236 – 249

14

Helix

253 – 259

7

Turn

260 – 262

3

Helix

265 – 291

27

Helix

295 – 322

28

Sequences

	Sequence		Length	Mass (Da)
	P00953-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: B8C4C6028F0913B0	FASTA	328	37,193
	10 20 30 40 50 60 MKTIFSGIQP SGVITIGNYI GALRQFVELQ HEYNCYFCIV DQHAITVWQD PHELRQNIRR 70 80 90 100 110 120 LAAKYLAVGI DPTQATLFIQ SEVPAHAQAA WMLQCIVYIG ELERMTQFKE KSAGKEAVSA 130 140 150 160 170 180 GLLTYPPLMA ADILLYNTDI VPVGEDQKQH IELTRDLAER FNKRYGELFT IPEARIPKVG 190 200 210 220 230 240 ARIMSLVDPT KKMSKSDPNP KAYITLLDDA KTIEKKIKSA VTDSEGTIRY DKEAKPGISN 250 260 270 280 290 300 LLNIYSTLSG QSIEELERQY EGKGYGVFKA DLAQVVIETL RPIQERYHHW MESEELDRVL 310 320 DEGAEKANRV ASEMVRKMEQ AMGLGRRR

References

[1]	"Cloning and complete nucleotide sequence of the Bacillus stearothermophilus tryptophanyl tRNA synthetase gene." Barstow D.A., Sharman A.F., Atkinson T., Minton N.P. Gene 46:37-45(1986) [PubMed: 3026925] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The amino acid sequence of tryptophanyl tRNA synthetase from Bacillus stearothermophilus." Winter G.P., Hartley B.S. FEBS Lett. 80:340-342(1977) [PubMed: 891985] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-327.
[3]	"Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase." Doublie S., Bricogne G., Gilmore C., Carter C.W. Jr. Structure 3:17-31(1995) [PubMed: 7743129] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[4]	"2.9-A crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site." Ilyin V.A., Temple B., Hu M., Li G.-P., Yin Y., Vachette P., Carter C.W. Jr. Protein Sci. 9:218-231(2000) [PubMed: 10716174] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M14742 Genomic DNA. Translation: AAA22873.1.

PIR

YWBSF. A26055.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D2R	X-ray	2.90	A/B/C/D/E/F	1-326	[»]
1I6K	X-ray	1.72	A	1-328	[»]
1I6L	X-ray	1.72	A	1-328	[»]
1I6M	X-ray	1.72	A	1-328	[»]
1M83	X-ray	2.20	A	1-328	[»]
1MAU	X-ray	2.15	A	1-328	[»]
1MAW	X-ray	3.00	A/B/C/D/E/F	1-328	[»]
1MB2	X-ray	2.70	A/B/C/D/E/F	1-328	[»]
2OV4	X-ray	2.50	A	1-328	[»]
3FHJ	X-ray	2.65	A/B/C/D/E/F	1-328	[»]
3FI0	X-ray	2.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R	1-326	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

6.1.1.2. 266715.

Family and domain databases

HAMAP

MF_00140.
[Tree]

InterPro

IPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ib.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-synth_Ib.
[Graphical view]

Gene3D

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

PANTHER

PTHR10055. Trp_tRNA-synt_1b. 1 hit.

Pfam

PF00579. tRNA-synt_1b. 1 hit.
[Graphical view]

PRINTS

PR01039. TRNASYNTHTRP.

TIGRFAMs

TIGR00233. trpS. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00150. L-Tryptophan.

Entry information

Entry name

SYW_BACST

Accession

Primary (citable) accession number: P00953

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1988
Last modified:	June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)