ID   FMT_RICFE               Reviewed;         303 AA.
AC   O33523; Q4UMN2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 122.
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=RF_0325;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61176.1; -; Genomic_DNA.
DR   EMBL; Y13131; CAA73598.1; -; Genomic_DNA.
DR   RefSeq; WP_011270669.1; NC_007109.1.
DR   AlphaFoldDB; O33523; -.
DR   SMR; O33523; -.
DR   STRING; 315456.RF_0325; -.
DR   EnsemblBacteria; AAY61176; AAY61176; RF_0325.
DR   KEGG; rfe:RF_0325; -.
DR   eggNOG; COG0223; Bacteria.
DR   HOGENOM; CLU_033347_1_1_5; -.
DR   OMA; CCPVVAY; -.
DR   OrthoDB; 2009156at2; -.
DR   Proteomes; UP000008548; 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_0000083030"
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"
FT   CONFLICT        250
FT                   /note="E -> D (in Ref. 2; CAA73598)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="Missing (in Ref. 2; CAA73598)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   303 AA;  34001 MW;  76D4A7B3ED056A63 CRC64;
     MKVIFMGTPE FAVPALKKLI THHEVKAVFA QQPKAKGRGL NLAKSPIHQL AFEHQIPVYT
     PSTLRNDKTI NLINKINADI IVVIAYGFIV PKAILEAKKY GCLNIHPSDL PRHRGAAPLQ
     RTIIEGDRKS SVCIMRMDAG LDTGDILMKE DFDLEERTTL EELHNKCANL GAELLIKTLA
     NIDNIVPIKQ SSDGVTYAHK LTKEEGKINW YESAYKIDCK IRGMNPWPGA YFSYNDKIIK
     ILEAEYLNAE HHFTSGTVIS DKLEIACGSG ILRVKKLQQE SKKALNIEEF LRGTNILKDT
     ILK