ID   FMT_MYCPN               Reviewed;         311 AA.
AC   P75235;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000250|UniProtKB:P23882};
DE            EC=2.1.2.9 {ECO:0000250|UniProtKB:P23882};
GN   Name=fmt; OrderedLocusNames=MPN_543; ORFNames=MP299;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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:0000250|UniProtKB:P23882}.
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:0000250|UniProtKB:P23882};
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000305}.
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DR   EMBL; U00089; AAB95947.1; -; Genomic_DNA.
DR   PIR; S73625; S73625.
DR   RefSeq; NP_110232.1; NC_000912.1.
DR   RefSeq; WP_010874900.1; NC_000912.1.
DR   AlphaFoldDB; P75235; -.
DR   SMR; P75235; -.
DR   STRING; 272634.MPN_543; -.
DR   EnsemblBacteria; AAB95947; AAB95947; MPN_543.
DR   KEGG; mpn:MPN_543; -.
DR   PATRIC; fig|272634.6.peg.605; -.
DR   HOGENOM; CLU_033347_1_1_14; -.
DR   OMA; CCPVVAY; -.
DR   BioCyc; MPNE272634:G1GJ3-893-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR   CDD; cd08704; Met_tRNA_FMT_C; 1.
DR   Gene3D; 3.10.25.10; -; 1.
DR   InterPro; IPR005794; Fmt.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR037022; Formyl_trans_C_sf.
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; Reference proteome; Transferase.
FT   CHAIN           1..311
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_0000082997"
FT   BINDING         109..112
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  34905 MW;  62D7958C19DAB6E9 CRC64;
     MIKVVFFGTS TLSKCCLEAI FQDPEFVVCG VVTQPDKVNE RNNKINFSAV KQFCIENNIP
     CFQPEKNIQI KTELAQLQAD IGVCVAFGQY IHNDIINLFP YKIANLHPSK LPLLRGGAPL
     HWTIINGFTT SSLSVIELVQ KMDAGPIWKQ KDFKVNPNWN TGDLFEYVQT HAPQFLIQCL
     KEIVSGKSQW KEQINPPTFG LNIKKEQERL DLNLEPKAFI NWVKGLAPKP GGWLEFEGQN
     IKILQATYLG KMTSTTAVGQ ITKISKQGIE IALANDEIVL LQIIQIPGKR AMGVSEIING
     KHPFAEGKFF H