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B7GUP8 (FMT_BIFLS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 34. 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:Blon_2133, BLIJ_2210
OrganismBifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) [Complete proteome] [HAMAP]
Taxonomic identifier391904 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length328 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 – 328328Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_1000190008

Regions

Region110 – 1134Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
B7GUP8 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: A80D765714D38A38

FASTA32834,747
        10         20         30         40         50         60 
MLKLVFAGTP DVAVPSLKAF ATDPRFDVVG VITRPDAPTG RGRKLTPSPV KAKALELGLP 

        70         80         90        100        110        120 
VIDLKPRSPE FMEALNDLHA DIAAVIAYGN ILPKNVLDAV PMGWYNLHFS NLPKWRGAAP 

       130        140        150        160        170        180 
AQRAIWAGDP TTGADVFKVG EGLDDGPIVA SLTIELTGRE TSGELLDRLA EEGAPMYVDA 

       190        200        210        220        230        240 
LAAVGEGTAT FTAQPAECLE YAHKITVEDA RISWTDEAGA IDRQIRACTP HPGAWTELFA 

       250        260        270        280        290        300 
EGPIADNDGS TAKSLTLHIL AAQPADQSNP NTPADLKPGE LKVGKKNVWV GTGSTPLELI 

       310        320 
QVKAQGKKAM RAADWARGAR LSPAACVR 

« Hide

References

[1]"The genome sequence of Bifidobacterium longum subsp. infantis reveals adaptations for milk utilization within the infant microbiome."
Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R., Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P., Richardson P.M., Mills D.A.
Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12.
[2]"Bifidobacteria can protect from enteropathogenic infection through production of acetate."
Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T., Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J., Morita H., Hattori M., Ohno H.
Nature 469:543-547(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001095 Genomic DNA. Translation: ACJ53194.1.
AP010889 Genomic DNA. Translation: BAJ69787.1.
RefSeqYP_002323572.1. NC_011593.1.
YP_005585957.1. NC_017219.1.

3D structure databases

ProteinModelPortalB7GUP8.
ModBaseSearch...

Protein-protein interaction databases

STRING391904.Blon_2133.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ53194; ACJ53194; Blon_2133.
BAJ69787; BAJ69787; BLIJ_2210.
GeneID12167863.
7054189.
KEGGbln:Blon_2133.
blon:BLIJ_2210.
PATRIC21125335. VBIBifLon71229_2145.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
ProtClustDBCLSK573224.

Enzyme and pathway databases

BioCycBLON391904:GCDR-2203-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.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMT_BIFLS
AccessionPrimary (citable) accession number: B7GUP8
Secondary accession number(s): E8MMY4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 29, 2013
This is version 34 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