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B8ZMJ8 (FMT_STRPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionyl-tRNA formyltransferase

EC=2.1.2.9
Gene names
Name:fmt
Ordered Locus Names:SPN23F17380
OrganismStreptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1) [Complete proteome] [HAMAP]
Taxonomic identifier561276 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length311 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)
   Molecular_functionmethionyl-tRNA formyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

methyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 311311Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_1000190044

Regions

Region110 – 1134Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
B8ZMJ8 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 96A9E4FE6FBF7316

FASTA31133,971
        10         20         30         40         50         60 
MTKLIFMGTP DFSATVLKGL LTDDRYEILA VVTQPDRAVG RKKVIQETPV KQAAKEAGLS 

        70         80         90        100        110        120 
IYQPEKLSGS PEMEELMKLG ADGIVTAAFG QFLPSKLLDS MDFAVNVHAS LLPRHRGGAP 

       130        140        150        160        170        180 
IHYALIQGDE EAGVTIMEMV KEMDAGDMIS RRSIPITDED NVGTLFEKLA LVGRDLLLDT 

       190        200        210        220        230        240 
LPAYIAGDIK PEPQDTSQVT FSPNIKPEEE KLDWNKTNRQ LFNQIRGMNP WPVAHAFLKG 

       250        260        270        280        290        300 
DRFKIYEALP VEGQGNPGEI LSIGKKELIV ATAEGALSLK QVQPAGKPKM DIASFLNGVG 

       310 
RTLTVGERFG D 

« Hide

References

[1]"Role of conjugative elements in the evolution of the multidrug-resistant pandemic clone Streptococcus pneumoniae Spain23F ST81."
Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C., Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D., Mitchell T.J.
J. Bacteriol. 191:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700669 / Spain 23F-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM211187 Genomic DNA. Translation: CAR69505.1.
RefSeqYP_002511621.1. NC_011900.1.

3D structure databases

ProteinModelPortalB8ZMJ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561276.SPN23F_17380.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR69505; CAR69505; SPN23F17380.
GeneID7329512.
KEGGsne:SPN23F_17380.
PATRIC19674852. VBIStrPne132160_1828.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
KOK00604.
OMAKAQAQNE.
OrthoDBEOG6B09WV.

Enzyme and pathway databases

BioCycSPNE561276:GJFJ-1665-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. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
PROSITEPS00373. GART. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMT_STRPJ
AccessionPrimary (citable) accession number: B8ZMJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: June 11, 2014
This is version 43 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