ID   FMT_BACVZ               Reviewed;         317 AA.
AC   A7Z4J3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=RBAM_015560;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS73919.1; -; Genomic_DNA.
DR   RefSeq; WP_012117531.1; NC_009725.2.
DR   AlphaFoldDB; A7Z4J3; -.
DR   SMR; A7Z4J3; -.
DR   STRING; 326423.RBAM_015560; -.
DR   EnsemblBacteria; ABS73919; ABS73919; RBAM_015560.
DR   KEGG; bay:RBAM_015560; -.
DR   HOGENOM; CLU_033347_1_1_9; -.
DR   OMA; CCPVVAY; -.
DR   Proteomes; UP000001120; 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   Gene3D; 3.10.25.10; -; 1.
DR   HAMAP; MF_00182; Formyl_trans; 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; IPR001555; GART_AS.
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.
DR   PROSITE; PS00373; GART; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis; Transferase.
FT   CHAIN           1..317
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_1000020017"
FT   REGION          292..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   317 AA;  34727 MW;  A925D14D6840270E CRC64;
     MTRIVFMGTP DFSVPVLRTL IEDGYEVVGV VTQPDRPKGR KKIMTPPPVK AEAERHGIPV
     LQPEKVRLEE EIEKVLSLKP DLIVTAAFGQ ILPKQLLDGP KYGCINVHAS LLPELRGGAP
     IHYSILQGKK KTGVTIMYMV EKLDAGDMIS KIEVEIDETD NVGTLHDKLS IAGAKLLSET
     VPNVISGNIK PIKQDESKAT YAPNIKREQE RIDWAKPGEE IYNQIRGLNP WPVAYTTLNG
     QNMKVWASEK VAAKTEAAPG TVIRTEQNGI VVASGNSTAL LITELQPAGK KRMKGEDFVR
     GKNVQPGDVL GEANEEN