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Q5WTK7 (FMT_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methionyl-tRNA formyltransferase

EC=2.1.2.9
Gene names
Name:fmt
Ordered Locus Names:lpl2517
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by: (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP By similarity. HAMAP-Rule MF_00182

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). HAMAP-Rule MF_00182

Sequence similarities

Belongs to the Fmt family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtranslational initiation

Inferred from electronic annotation. Source: GOC

   Molecular_functionmethionyl-tRNA formyltransferase activity

Inferred from electronic annotation. Source: HAMAP

methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_0000082983

Regions

Region112 – 1154Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WTK7 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 9E045738412CC9DC

FASTA31434,364
        10         20         30         40         50         60 
MNGLTVVFAG TPEFGLPCLD ALIQSRHHLK AVYTQPDRPA GRGRKLQESP VKEWAINHQI 

        70         80         90        100        110        120 
SVYQPLNFKN QEAVDELSAL KPDVMVVIAY GLILPKAVLE IPRLGCINVH ASLLPRWRGA 

       130        140        150        160        170        180 
SPIQHAILHG DAESGVTIMQ MDVGLDTGPM LCKAACPVTS SDTAGSLHDK LAKMSVKPLL 

       190        200        210        220        230        240 
DVLEALASNS AQFELQNNEL ATYAGKINKE EARINWHQSA VEIDRKIRAF NPWPVAYTLA 

       250        260        270        280        290        300 
GELMLRIHQA KATDIMSTEM PGMVLNIDKT GMLVATSDNA LLVEKIQFPG AKVISVRDWL 

       310 
NSGKTQLHTG LMLQ 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH16757.1.
RefSeqYP_127846.1. NC_006369.1.

3D structure databases

ProteinModelPortalQ5WTK7.
ModBaseSearch...

Protein-protein interaction databases

STRING297245.lpl2517.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH16757; CAH16757; lpl2517.
GeneID3115954.
KEGGlpf:lpl2517.
PATRIC22318911. VBILegPne33733_2764.

Organism-specific databases

LegioListlpl2517.
CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAGITLMQM.
ProtClustDBCLSK833498.

Enzyme and pathway databases

BioCycLPNE297245:GJD4-2727-MONOMER.

Family and domain databases

Gene3D3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPMF_00182. Formyl_trans.
InterProIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERPTHR11138. PTHR11138. 1 hit.
PfamPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMSSF50486. FMT_C_like. 1 hit.
SSF53328. formyl_transf. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
PROSITEPS00373. GART. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMT_LEGPL
AccessionPrimary (citable) accession number: Q5WTK7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: November 23, 2004
Last modified: May 29, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families