FMT_RICPU
ID FMT_RICPU Reviewed; 303 AA.
AC C4K0Y8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=RPR_01885;
OS Rickettsia peacockii (strain Rustic).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=562019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rustic;
RX PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT with virulent Rickettsia rickettsii: identification of virulence factors.";
RL PLoS ONE 4:E8361-E8361(2009).
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; CP001227; ACR47239.1; -; Genomic_DNA.
DR RefSeq; WP_012736517.1; NC_012730.1.
DR AlphaFoldDB; C4K0Y8; -.
DR SMR; C4K0Y8; -.
DR EnsemblBacteria; ACR47239; ACR47239; RPR_01885.
DR KEGG; rpk:RPR_01885; -.
DR HOGENOM; CLU_033347_1_1_5; -.
DR OMA; CCPVVAY; -.
DR Proteomes; UP000005015; 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_1000203875"
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; 33971 MW; E0967EC4A601F626 CRC64;
MKVIFMGTPE FAVPALKKLI THHEVKAVFT QQPKAKGRGL NLAKSPIHQL AFEHQIPVYT
PSTLRNDEII NLINKVNADI IVVIAYGFIV PKAILEAKKY GCLNIHPSDL PRHRGAAPLQ
RTIIEGDRKS SVCIMRMDTG LDTGDILMKE DFDLEERITL EELHNKCANL GAELLIKTLA
NIDNIVPITQ PSDGVTYAHK LTKAEGKINW HESAYKIDCK IRGMNPWPGV YFSYNDKIIK
ILEAEYLNAD HHFTSGTVIS DKLEIACGSG ILRVKKLQQE SKKALNIEEF LRGTNILKDT
VLK
