ID   FMT_UREP2               Reviewed;         305 AA.
AC   B1AJA4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000255|HAMAP-Rule:MF_00182};
DE            EC=2.1.2.9 {ECO:0000255|HAMAP-Rule:MF_00182};
GN   Name=fmt {ECO:0000255|HAMAP-Rule:MF_00182}; OrderedLocusNames=UPA3_0482;
OS   Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=505682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA   Methe B.A., Glass J., Waites K., Shrivastava S.;
RT   "Genome sequence of Ureaplasma parvum serovar 3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Attaches a formyl group to the free amino group of methionyl-
CC       tRNA(fMet). The formyl group appears to play a dual role in the
CC       initiator identity of N-formylmethionyl-tRNA by promoting its
CC       recognition by IF2 and preventing the misappropriation of this tRNA by
CC       the elongation apparatus. {ECO:0000255|HAMAP-Rule:MF_00182}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) =
CC         (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-
CC         tRNA(fMet); Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-
CC         COMP:9953, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC         ChEBI:CHEBI:78530, ChEBI:CHEBI:78844; EC=2.1.2.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00182};
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000255|HAMAP-
CC       Rule:MF_00182}.
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DR   EMBL; CP000942; ACA32879.1; -; Genomic_DNA.
DR   RefSeq; WP_010891782.1; NC_010503.1.
DR   AlphaFoldDB; B1AJA4; -.
DR   SMR; B1AJA4; -.
DR   EnsemblBacteria; ACA32879; ACA32879; UPA3_0482.
DR   GeneID; 29672150; -.
DR   KEGG; upa:UPA3_0482; -.
DR   HOGENOM; CLU_033347_1_1_14; -.
DR   OMA; CCPVVAY; -.
DR   OrthoDB; 2009156at2; -.
DR   Proteomes; UP000002162; Chromosome.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR   CDD; cd08704; Met_tRNA_FMT_C; 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; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR   InterPro; IPR044135; Met-tRNA-FMT_C.
DR   InterPro; IPR041711; Met-tRNA-FMT_N.
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.
PE   3: Inferred from homology;
KW   Protein biosynthesis; Transferase.
FT   CHAIN           1..305
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_1000077330"
FT   BINDING         110..113
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   305 AA;  34793 MW;  54E5676DE3291240 CRC64;
     MKYKVMFFGT PEIAKIVLET LFNMHEVDLI AVVSQPDAHF DRKKNVIYSP VKQFCLDHNI
     KLFQPEKIKE IEEEIRILGP DIIITCAFGQ FINQGIIDIP KYKIVNIHAS LLPKLRGGAP
     IHYAILNGEL KTGITLMHTI KKMDAGNILF QRSLEINDCT TTKSLTLELA NLSALMIKEH
     FLELVKPNLV GIQQDENSVS FAYNIQKDQN IINFDQPAFF INRFVNAMYD KPIAIMQYNG
     VSIKVYQVKI TNQKSCQKPG TIMIFKNQLF VSTQDFDIEL LLIQLPNKKP LSPKVLLNGK
     NPFIN