FMT_RICPR
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 03-AUG-2022, entry version 120.
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; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC 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=(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; AJ235270; CAA14674.1; -; Genomic_DNA.
DR EMBL; Z49077; CAA88897.1; -; Genomic_DNA.
DR PIR; C71732; C71732.
DR RefSeq; NP_220597.1; NC_000963.1.
DR RefSeq; WP_010886235.1; NC_000963.1.
DR AlphaFoldDB; P50932; -.
DR SMR; P50932; -.
DR STRING; 272947.RP209; -.
DR PRIDE; P50932; -.
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 OMA; CCPVVAY; -.
DR Proteomes; UP000002480; 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; 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
