ID FMT_STAEQ Reviewed; 310 AA.
AC Q5HPX5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 01-MAY-2013, entry version 60.
DE RecName: Full=Methionyl-tRNA formyltransferase;
DE EC=2.1.2.9;
GN Name=fmt; OrderedLocusNames=SERP0782;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA Hance I.R., Nelson K.E., Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete
RT genome analysis of an early methicillin-resistant Staphylococcus
RT aureus strain and a biofilm-producing methicillin-resistant
RT Staphylococcus epidermidis strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW54200.1; -; Genomic_DNA.
DR RefSeq; YP_188365.1; NC_002976.3.
DR ProteinModelPortal; Q5HPX5; -.
DR STRING; 176279.SERP0782; -.
DR EnsemblBacteria; AAW54200; AAW54200; SERP0782.
DR GeneID; 3241559; -.
DR KEGG; ser:SERP0782; -.
DR PATRIC; 19612435; VBIStaEpi130894_0760.
DR eggNOG; COG0223; -.
DR HOGENOM; HOG000261177; -.
DR KO; K00604; -.
DR OMA; DWNKSAR; -.
DR ProtClustDB; CLSK885209; -.
DR BioCyc; SEPI176279:GJJB-808-MONOMER; -.
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_0000083052.
FT REGION 109 112 Tetrahydrofolate (THF) binding (By
FT similarity).
SQ SEQUENCE 310 AA; 34101 MW; 268C680D348F605B CRC64;
MSKIIFMGTP DFSTKVLEML IAEHEVIAVV TQPDRPVGRK KVMTPPPVKR VATKHQIPVY
QPEKLKDSQE LDVLLSLESD LIVTAAFGQL LPESLLNAPK LGAINVHASL LPKYRGGAPI
HQAIIDGEEE TGITIMYMVK KLDAGNIISQ QSIRIEEEDN VGTMHDKLSF LGAELLKKTL
PSIIDNTNDS IPQDDALATF ASNIRREDER IDWNMSAQAI HNHIRGLSPW PVAYTTMNEK
NLKLFSAFIV KGKKGNPGTI IEATKHELII ATGSDDAIAL TEIQPAGKKR MKVTDYLSGV
QESLVGKVLL
//
