ID   FMT_LATSS               Reviewed;         318 AA.
AC   Q38XT6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=LCA_0689;
OS   Latilactobacillus sakei subsp. sakei (strain 23K) (Lactobacillus sakei
OS   subsp. sakei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Latilactobacillus.
OX   NCBI_TaxID=314315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23K;
RX   PubMed=16273110; DOI=10.1038/nbt1160;
RA   Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M.,
RA   Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V.,
RA   Zagorec M.;
RT   "The complete genome sequence of the meat-borne lactic acid bacterium
RT   Lactobacillus sakei 23K.";
RL   Nat. Biotechnol. 23:1527-1533(2005).
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; CR936503; CAI54993.1; -; Genomic_DNA.
DR   RefSeq; WP_011374398.1; NC_007576.1.
DR   AlphaFoldDB; Q38XT6; -.
DR   SMR; Q38XT6; -.
DR   STRING; 314315.LCA_0689; -.
DR   EnsemblBacteria; CAI54993; CAI54993; LCA_0689.
DR   KEGG; lsa:LCA_0689; -.
DR   eggNOG; COG0223; Bacteria.
DR   HOGENOM; CLU_033347_1_1_9; -.
DR   OMA; CCPVVAY; -.
DR   OrthoDB; 2009156at2; -.
DR   BioCyc; LSAK314315:LCA_RS03485-MON; -.
DR   Proteomes; UP000002707; 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; 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..318
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_1000020090"
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   318 AA;  34283 MW;  37034369ECC68DFB CRC64;
     MTSIVFMGTP QFSVPILEAL VANDYQILAV VTQPDRKVGR KQVLQQTPVK EAAVRLDLPV
     FQPEKLSGSP ELADVIALQP DLIVTAAYGQ FLPTKLLEAA KIAAINVHGS LLPKYRGGAP
     IQYAVLNGDS EIGITIMHMA KKMDAGDMIE QASIPIEATD DTGSLFDKLS YVGRDLLLKT
     LPGIIAQTAP RTPQDEVQVT FAYNITKEQE QLDINQPAEQ LLNQIRALRP QPGAWLAVNG
     QRTKIWQATV AETTTDQAAG VVVALNKKDF ELAAGNGTVL KITEIQPAGK AKMPVQSYLN
     GVGKQLAVGQ QVVVQDAE