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Protein

Tryptophan--tRNA ligase

Gene

trpS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei198 – 1981ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • tryptophan-tRNA ligase activity Source: EcoCyc

GO - Biological processi

  • tryptophanyl-tRNA aminoacylation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:TRPS-MONOMER.
ECOL316407:JW3347-MONOMER.
MetaCyc:TRPS-MONOMER.
SABIO-RKP00954.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan--tRNA ligase (EC:6.1.1.2)
Alternative name(s):
Tryptophanyl-tRNA synthetase
Short name:
TrpRS
Gene namesi
Name:trpS
Ordered Locus Names:b3384, JW3347
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11030. trpS.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Tryptophan--tRNA ligasePRO_0000136628Add
BLAST

Proteomic databases

EPDiP00954.
PaxDbiP00954.
PRIDEiP00954.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4259293. 156 interactions.
DIPiDIP-11042N.
IntActiP00954. 12 interactions.
MINTiMINT-1244806.
STRINGi511145.b3384.

Structurei

3D structure databases

ProteinModelPortaliP00954.
SMRiP00954. Positions 3-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi12 – 209"HIGH" region
Motifi195 – 1995"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C31. Bacteria.
COG0180. LUCA.
HOGENOMiHOG000059940.
InParanoidiP00954.
KOiK01867.
OMAiGWGQFKP.
OrthoDBiEOG686NJQ.
PhylomeDBiP00954.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00140_B. Trp_tRNA_synth_B.
InterProiIPR001412. 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]
PANTHERiPTHR10055. PTHR10055. 1 hit.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01039. TRNASYNTHTRP.
TIGRFAMsiTIGR00233. trpS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00954-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKPIVFSGA QPSGELTIGN YMGALRQWVN MQDDYHCIYC IVDQHAITVR
60 70 80 90 100
QDAQKLRKAT LDTLALYLAC GIDPEKSTIF VQSHVPEHAQ LGWALNCYTY
110 120 130 140 150
FGELSRMTQF KDKSARYAEN INAGLFDYPV LMAADILLYQ TNLVPVGEDQ
160 170 180 190 200
KQHLELSRDI AQRFNALYGE IFKVPEPFIP KSGARVMSLL EPTKKMSKSD
210 220 230 240 250
DNRNNVIGLL EDPKSVVKKI KRAVTDSDEP PVVRYDVQNK AGVSNLLDIL
260 270 280 290 300
SAVTGQSIPE LEKQFEGKMY GHLKGEVADA VSGMLTELQE RYHRFRNDEA
310 320 330
FLQQVMKDGA EKASAHASRT LKAVYEAIGF VAKP
Length:334
Mass (Da):37,438
Last modified:August 29, 2003 - v3
Checksum:iCBAC73ABB8406026
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301N → K (PubMed:7042706).Curated
Sequence conflicti30 – 301N → K (PubMed:7603433).Curated
Sequence conflicti326 – 3261E → Q (PubMed:7042706).Curated
Sequence conflicti326 – 3261E → Q (PubMed:7603433).Curated
Sequence conflicti334 – 3341P → R (PubMed:7042706).Curated
Sequence conflicti334 – 3341P → R (PubMed:7603433).Curated
Sequence conflicti334 – 3341P → R (PubMed:8555191).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601T → R in TRPS567C; reduced activity, thermolabile.
Natural varianti91 – 911L → F in TRPS10330; reduced activity.
Natural varianti112 – 1121D → E in TRPS9969; no effect in activity.
Natural varianti129 – 1291P → S in TRPS9969; reduced activity.
Natural varianti133 – 1331A → E in TRPS42C; reduced activity.
Natural varianti196 – 1961M → I in TRPS271C; activity largely reduced.
Natural varianti329 – 3291G → S in TRPS4040; reduced activity.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00371 Genomic DNA. Translation: CAA23670.1.
Z19601 Genomic DNA. Translation: CAA79669.1.
U38647 Genomic DNA. Translation: AAA92300.1.
U18997 Genomic DNA. Translation: AAA58181.1.
U00096 Genomic DNA. Translation: AAC76409.1.
AP009048 Genomic DNA. Translation: BAE77907.1.
PIRiC65133. YWEC.
RefSeqiNP_417843.1. NC_000913.3.
WP_000165552.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76409; AAC76409; b3384.
BAE77907; BAE77907; BAE77907.
GeneIDi947894.
KEGGiecj:JW3347.
eco:b3384.
PATRICi32122200. VBIEscCol129921_3477.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00371 Genomic DNA. Translation: CAA23670.1.
Z19601 Genomic DNA. Translation: CAA79669.1.
U38647 Genomic DNA. Translation: AAA92300.1.
U18997 Genomic DNA. Translation: AAA58181.1.
U00096 Genomic DNA. Translation: AAC76409.1.
AP009048 Genomic DNA. Translation: BAE77907.1.
PIRiC65133. YWEC.
RefSeqiNP_417843.1. NC_000913.3.
WP_000165552.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP00954.
SMRiP00954. Positions 3-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259293. 156 interactions.
DIPiDIP-11042N.
IntActiP00954. 12 interactions.
MINTiMINT-1244806.
STRINGi511145.b3384.

Proteomic databases

EPDiP00954.
PaxDbiP00954.
PRIDEiP00954.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76409; AAC76409; b3384.
BAE77907; BAE77907; BAE77907.
GeneIDi947894.
KEGGiecj:JW3347.
eco:b3384.
PATRICi32122200. VBIEscCol129921_3477.

Organism-specific databases

EchoBASEiEB1023.
EcoGeneiEG11030. trpS.

Phylogenomic databases

eggNOGiENOG4105C31. Bacteria.
COG0180. LUCA.
HOGENOMiHOG000059940.
InParanoidiP00954.
KOiK01867.
OMAiGWGQFKP.
OrthoDBiEOG686NJQ.
PhylomeDBiP00954.

Enzyme and pathway databases

BioCyciEcoCyc:TRPS-MONOMER.
ECOL316407:JW3347-MONOMER.
MetaCyc:TRPS-MONOMER.
SABIO-RKP00954.

Miscellaneous databases

PROiP00954.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00140_B. Trp_tRNA_synth_B.
InterProiIPR001412. 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]
PANTHERiPTHR10055. PTHR10055. 1 hit.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01039. TRNASYNTHTRP.
TIGRFAMsiTIGR00233. trpS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of the structural gene for Escherichia coli tryptophanyl-tRNA synthetase."
    Hall C.V., van Cleemput M., Muench K.H., Yanofsky C.
    J. Biol. Chem. 257:6132-6136(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Characterization of three genes in the dam-containing operon of Escherichia coli."
    Lyngstadaas A., Lobner-Olesen A., Boye E.
    Mol. Gen. Genet. 247:546-554(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Escherichia coli tryptophanyl-tRNA synthetase mutants selected for tryptophan auxotrophy implicate the dimer interface in optimizing amino acid binding."
    Sever S., Rogers K., Rogers M.J., Carter C. Jr., Soell D.
    Biochemistry 35:32-40(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Sequence homologies between the tryptophanyl tRNA synthetases of Bacillus stearothermophilus and Escherichia coli."
    Winter G.P., Hartley B.S., McLachlan A.D., Lee M., Muench K.H.
    FEBS Lett. 82:348-350(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: CONFIRMS PROTEIN SEQUENCE BY AMINO ACID ANALYSIS.
  7. "Cloning and characterization of the gene for Escherichia coli tryptophanyl-transfer ribonucleic acid synthetase."
    Hall C.V., Yanofsky C.
    J. Bacteriol. 148:941-949(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11 AND 152-171.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiSYW_ECOLI
AccessioniPrimary (citable) accession number: P00954
Secondary accession number(s): Q2M749
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 29, 2003
Last modified: April 13, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.