ID FMT_STAES Reviewed; 310 AA.
AC Q8CSW1;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 01-MAY-2013, entry version 72.
DE RecName: Full=Methionyl-tRNA formyltransferase;
DE EC=2.1.2.9;
GN Name=fmt; OrderedLocusNames=SE_0891;
OS Staphylococcus epidermidis (strain ATCC 12228).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- FUNCTION: Modifies the free amino group of the aminoacyl moiety of
CC methionyl-tRNA(fMet). The formyl group appears to play a dual role
CC in the initiator identity of N-formylmethionyl-tRNA by: (I)
CC promoting its recognition by IF2 and (II) impairing its binding to
CC EFTu-GTP (By similarity).
CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl-
CC tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).
CC -!- SIMILARITY: Belongs to the fmt family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AE015929; AAO04488.1; -; Genomic_DNA.
DR RefSeq; NP_764446.1; NC_004461.1.
DR ProteinModelPortal; Q8CSW1; -.
DR STRING; 176280.SE0891; -.
DR EnsemblBacteria; AAO04488; AAO04488; SE_0891.
DR GeneID; 1056897; -.
DR KEGG; sep:SE0891; -.
DR PATRIC; 19607581; VBIStaEpi113981_0864.
DR eggNOG; COG0223; -.
DR KO; K00604; -.
DR OMA; DWNKSAR; -.
DR ProtClustDB; CLSK885209; -.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:HAMAP.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006413; P:translational initiation; IEA:GOC.
DR Gene3D; 3.10.25.10; -; 1.
DR Gene3D; 3.40.50.170; -; 1.
DR HAMAP; MF_00182; Formyl_trans; 1; -.
DR InterPro; IPR005794; Fmt.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR011034; Formyl_transferase_C-like.
DR InterPro; IPR001555; GART_AS.
DR InterPro; IPR015518; Met_tRNA_Form_TA-like.
DR PANTHER; PTHR11138; PTHR11138; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF50486; FMT_C_like; 1.
DR SUPFAM; SSF53328; formyl_transf; 1.
DR TIGRFAMs; TIGR00460; fmt; 1.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
KW Complete proteome; Methyltransferase; Protein biosynthesis;
KW Transferase.
FT CHAIN 1 310 Methionyl-tRNA formyltransferase.
FT /FTId=PRO_0000083051.
FT REGION 109 112 Tetrahydrofolate (THF) binding (By
FT similarity).
SQ SEQUENCE 310 AA; 34133 MW; 9498818D503F1CD3 CRC64;
MSKIIFMGTP DFSTKILEML IAEHEVIAVV TQPDRPVGRK KVMTPPPVKR VATKHQIPVY
QPEKLKDSQE LESLLSLESD LIVTAAFGQL LPESLLNAPK LGAINVHASL LPKYRGGAPI
HQAIIDGEEE TGITIMYMVK KLDAGNIISQ QSIRIEEEDN VGTMHDKLSF LGAELLKKTL
PSIIDNTNDS IPQDDALATF ASNIRREDER VDWNMSAQAI HNHIRGLSPW PVAYTTMNEK
NLKLFSAFIV KGKKGNPGTI IETTKHELII ATGSDDAIAL TEIQPAGKKR MKVTDYLSGV
QESLVGKVLL
//
