FMT_RICTY
ID FMT_RICTY Reviewed; 303 AA.
AC O33582; Q68XG0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 121.
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=RT0198;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU03682.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017197; AAU03682.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y13133; CAA73600.1; -; Genomic_DNA.
DR RefSeq; WP_011190669.1; NC_006142.1.
DR AlphaFoldDB; O33582; -.
DR SMR; O33582; -.
DR STRING; 257363.RT0198; -.
DR EnsemblBacteria; AAU03682; AAU03682; RT0198.
DR KEGG; rty:RT0198; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_1_5; -.
DR OMA; CCPVVAY; -.
DR OrthoDB; 2009156at2; -.
DR Proteomes; UP000000604; 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_0000083037"
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; 33913 MW; 536F48A4CFDFE38F CRC64;
MKVIFMGTPE FAVPTLKKLI IHHEVKAVFT QQPKAKGRGL YLAKSPIHQL AFEHQIPVYS
PSTLRNDETI NLINKVDADI IVVIAYGFIV PKAILEAKKY GCLNIHPSDL PRHRGAAPLQ
RTIIEGDLKS SVCIMRMDSG LDTGDILLKE DLNLEKRITL DELSNRCAHL GAELLIQTLA
NIDNIVPVKQ SSNGVTYAHK LTKAEGKINW YESAYSIDCK IRGMNPWPGA YFSYNDKIIK
ILEAEYLNYN HHFIPGTVIS NKLEIACGSG ILRVTKLQQE SKKALNIEAF LRGTNILKDT
ILK
