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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Staphylococcus aureus (strain MRSA252)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).UniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciSAUR282458:GJA5-1195-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferaseUniRule annotation (EC:2.1.2.9UniRule annotation)
Gene namesi
Name:fmtUniRule annotation
Ordered Locus Names:SAR1192
OrganismiStaphylococcus aureus (strain MRSA252)
Taxonomic identifieri282458 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 311311Methionyl-tRNA formyltransferasePRO_0000083048Add
BLAST

Proteomic databases

PRIDEiQ6GHL9.

Structurei

3D structure databases

ProteinModelPortaliQ6GHL9.
SMRiQ6GHL9. Positions 1-310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 1124Tetrahydrofolate (THF) bindingUniRule annotation

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.
OrthoDBiEOG6B09WV.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6GHL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKIIFMGTP DFSTTVLEML IAEHDVIAVV TQPDRPVGRK RVMTPPPVKK
60 70 80 90 100
VAMKYDLPVY QPEKLSGSEE LEQLLQLDVD LIVTAAFGQL LPESLLALPK
110 120 130 140 150
LGAINVHASL LPKYRGGAPI HQAIIDGEQE TGITIMYMVK KLDAGNIISQ
160 170 180 190 200
QAIKIEENDN VGTMHDKLSV LGADLLKETL PSIIEGTNES VPQDDTQATF
210 220 230 240 250
ASNIRREDER ISWNKPGRQV FNQIRGLSPW PVAYTTMDDT NLKIYDAELV
260 270 280 290 300
ETNKINEPGT IIETTKKAII VATNDNEAVA IKDMQLAGKK RMLAANYLSG
310
AQNTLVGKKL I
Length:311
Mass (Da):34,226
Last modified:July 19, 2004 - v1
Checksum:i0E40873B5F31867C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG40194.1.
RefSeqiWP_000161291.1. NC_002952.2.

Genome annotation databases

EnsemblBacteriaiCAG40194; CAG40194; SAR1192.
KEGGisar:SAR1192.
PATRICi19545931. VBIStaAur71814_1195.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG40194.1.
RefSeqiWP_000161291.1. NC_002952.2.

3D structure databases

ProteinModelPortaliQ6GHL9.
SMRiQ6GHL9. Positions 1-310.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ6GHL9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG40194; CAG40194; SAR1192.
KEGGisar:SAR1192.
PATRICi19545931. VBIStaAur71814_1195.

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.
OrthoDBiEOG6B09WV.

Enzyme and pathway databases

BioCyciSAUR282458:GJA5-1195-MONOMER.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MRSA252.

Entry informationi

Entry nameiFMT_STAAR
AccessioniPrimary (citable) accession number: Q6GHL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: July 19, 2004
Last modified: May 11, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. 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.