ID   FMT_RICPR               Reviewed;         303 AA.
AC   P50932;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   28-JAN-2026, entry version 132.
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=RP209;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-303.
RC   STRAIN=Madrid E;
RX   PubMed=7608097; DOI=10.1128/jb.177.14.4171-4175.1995;
RA   Andersson S.G.E., Zomorodipour A., Winkler H.H., Kurland C.G.;
RT   "Unusual organization of the rRNA genes in Rickettsia prowazekii.";
RL   J. Bacteriol. 177:4171-4175(1995).
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=L-methionyl-tRNA(fMet) + (6R)-10-formyltetrahydrofolate = N-
CC         formyl-L-methionyl-tRNA(fMet) + (6S)-5,6,7,8-tetrahydrofolate + H(+);
CC         Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-COMP:9953,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:78844, ChEBI:CHEBI:195366; 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, ECO:0000305}.
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DR   EMBL; AJ235270; CAA14674.1; -; Genomic_DNA.
DR   EMBL; Z49077; CAA88897.1; -; Genomic_DNA.
DR   PIR; C71732; C71732.
DR   RefSeq; WP_010886235.1; NC_000963.1.
DR   AlphaFoldDB; P50932; -.
DR   SMR; P50932; -.
DR   STRING; 272947.gene:17555290; -.
DR   EnsemblBacteria; CAA14674; CAA14674; CAA14674.
DR   GeneID; 57569337; -.
DR   KEGG; rpr:RP209; -.
DR   PATRIC; fig|272947.5.peg.218; -.
DR   eggNOG; COG0223; Bacteria.
DR   HOGENOM; CLU_033347_1_1_5; -.
DR   OrthoDB; 9802815at2; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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; 3.40.50.12230; -; 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   NCBIfam; TIGR00460; fmt; 1.
DR   PANTHER; PTHR11138; METHIONYL-TRNA FORMYLTRANSFERASE; 1.
DR   PANTHER; PTHR11138:SF5; METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..303
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_0000083033"
FT   BINDING         108..111
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   303 AA;  34159 MW;  2238362E782566ED CRC64;
     MKVIFMGTPE FAVPTLKKLI IHHEVKAVFT QQPKAKGRGL HLAKSPIHQL AFEHQIPVYS
     PSTLRNDETI NLIKKIDADI IVVIAYGFIV PKAILEAKKY GCLNIHPSDL PRHRGAAPLQ
     RTIIEGDRKS SVCIMRMDSG LDTGDILLKE DLNLERRITL DELSNKCAHL GAELLIKTLA
     NIDNIVPIKQ SSNGITYAHK LTKAEGKINW YESAYSIDCK IRGMNPWPGA YFSYNDKIIK
     ILRAEYFNYN HHFIPGTVIN NKLEIACGSG ILRVKKLQQE SKKALNIEEF LRGTNILKDT
     ILK
//