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Database: UniProt
Entry: Q8CSW1
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Original site: Q8CSW1 
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   16-APR-2014, entry version 78.
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.
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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; VRGMNPF; -.
DR   OrthoDB; EOG6B09WV; -.
DR   ProtClustDB; CLSK885209; -.
DR   BioCyc; SEPI176280:GCDG-897-MONOMER; -.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
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; SSF50486; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   TIGRFAMs; TIGR00460; fmt; 1.
DR   PROSITE; PS00373; GART; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Protein biosynthesis; 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
//
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