Q9PIB4 (SYW_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan--tRNA ligase
EC=6.1.1.2

Alternative name(s):
Tryptophanyl-tRNA synthetase
Short name=TrpRS

Gene names

Name:	trpS
Ordered Locus Names:	Cj0388

Organism

Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]

Taxonomic identifier

192222 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter › Campylobacter jejuni › Campylobacter jejuni subsp. jejuni

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp). HAMAP-Rule MF_00140
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
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 Complete proteome Reference proteome
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 – 319

319

Tryptophan--tRNA ligase HAMAP-Rule MF_00140

PRO_0000136613

Regions

Motif

9 – 17

9

"HIGH" region HAMAP-Rule MF_00140

Motif

189 – 193

5

"KMSKS" region HAMAP-Rule MF_00140

Sites

Binding site

192

1

ATP By similarity

Secondary structure

1

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319

Helix Strand Turn

Details...

Beta strand

3 – 7

5

Helix

15 – 20

6

Helix

22 – 27

6

Turn

28 – 31

4

Beta strand

35 – 38

4

Helix

40 – 43

4

Turn

44 – 46

3

Helix

50 – 66

17

Turn

71 – 73

3

Beta strand

74 – 78

5

Helix

79 – 81

3

Helix

84 – 92

9

Helix

93 – 95

3

Helix

98 – 102

5

Helix

105 – 112

8

Helix

119 – 134

16

Beta strand

138 – 141

4

Helix

144 – 146

3

Helix

147 – 164

18

Beta strand

172 – 174

3

Beta strand

187 – 189

3

Helix

192 – 194

3

Beta strand

199 – 201

3

Helix

204 – 212

9

Helix

227 – 229

3

Helix

231 – 236

6

Helix

237 – 239

3

Helix

242 – 254

13

Helix

259 – 273

15

Helix

275 – 286

12

Helix

288 – 317

30

Sequences

	Sequence		Length	Mass (Da)
	Q9PIB4 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: CB620B2B67AA6666	FASTA	319	36,084
	10 20 30 40 50 60 MRVLTGLQPS GDLHIGNYFG AIKQMVDAQE KSQMFMFIAN YHAMTSSQDG EKLKQNSLKA 70 80 90 100 110 120 AAAFLSLGID PQKSVFWLQS DVKEVMELYW ILSQFTPMGL LERAHSYKDK VAKGLSASHG 130 140 150 160 170 180 LFSYPVLMAA DILLFDTRIV PVGKDQIQHV EIARDIALKV NNEWGEIFTL PEARVNEEVA 190 200 210 220 230 240 VVVGTDGAKM SKSYQNTIDI FSSEKTLKKQ ISSIVTDSTA LEDPKDHENC NIFKIAKLFL 250 260 270 280 290 300 DESGQKELQI RYEKGGEGYG HFKIYLNELV NAYFKEAREK YNELLEKPSH LKEILDFGAT 310 KARKIAQEKM QKIYEKIGL

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL111168 Genomic DNA. Translation: CAL34538.1.

PIR

B81382.

RefSeq

YP_002343825.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3M5W	X-ray	2.32	A/B	1-319	[»]
3TZL	X-ray	2.15	A/B	1-319	[»]

ProteinModelPortal

Q9PIB4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9PIB4. 3 interactions.

STRING

192222.Cj0388.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAL34538; CAL34538; Cj0388.

GeneID

904711.

KEGG

cje:Cj0388.

PATRIC

20057691. VBICamJej33762_0379.

Phylogenomic databases

eggNOG

COG0180.

HOGENOM

HOG000059939.

KO

K01867.

OMA

SVDKNVE.

ProtClustDB

PRK00927.

Enzyme and pathway databases

BioCyc

CJEJ192222:GJTS-364-MONOMER.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

HAMAP

MF_00140_B. Trp_tRNA_synth_B.

InterPro

IPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-ligase.
IPR024109. Trp-tRNA-ligase_bac-type.
[Graphical view]

PANTHER

PTHR10055. PTHR10055. 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

EvolutionaryTrace

Q9PIB4.

Entry information

Entry name

SYW_CAMJE

Accession

Primary (citable) accession number: Q9PIB4
Secondary accession number(s): Q0PBC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program