ID   FMT_RICCN               Reviewed;         303 AA.
AC   O33519;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   03-AUG-2022, entry version 126.
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=RC0279;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-303.
RA   Andersson S.G.E., Stothard D.R., Romedenne M., Viseur N., Fuerst P.,
RA   Kurland C.G.;
RT   "Rearrangement of the rRNA genes in Rickettsia preceeded the divergence of
RT   the typhus and the spotted fever group Rickettsia.";
RL   Submitted (MAY-1997) 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, ECO:0000305}.
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DR   EMBL; AE006914; AAL02817.1; -; Genomic_DNA.
DR   EMBL; Y13122; CAA73589.1; -; Genomic_DNA.
DR   PIR; G97734; G97734.
DR   RefSeq; WP_010976939.1; NC_003103.1.
DR   AlphaFoldDB; O33519; -.
DR   SMR; O33519; -.
DR   EnsemblBacteria; AAL02817; AAL02817; RC0279.
DR   KEGG; rco:RC0279; -.
DR   PATRIC; fig|272944.4.peg.319; -.
DR   HOGENOM; CLU_033347_1_1_5; -.
DR   OMA; CCPVVAY; -.
DR   Proteomes; UP000000816; 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..303
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_0000083029"
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;  34001 MW;  51C4B3491E5ED14C CRC64;
     MKVIFMGTPE FAVPALKKLI THHEVKAVFT QQPKAKGRGL NLAKSPIHQL AFEHQIPVYT
     PSTLRNDEII NLINKVNADI IVVIAYGFIV PKAILEAKKY GCLNIHPSDL PRHRGAAPLQ
     RTIIEGDRKS SVCIMRMDTG LDTGDILMKE DFDLEERITL EELHNKCANL GAELLIKTLA
     NIDNIVPITQ PSDGVTYAHK LTKEEGKINW HESAYKIDCK IRGMNPWPGA YFSYNDKIIK
     ILEAEYLNAD HHFTSGTVIS DKLEIACGSG ILRVKKLQQE SKKALNIEEF LRGTNILKDT
     VLK