FMT_ECO57
ID FMT_ECO57 Reviewed; 315 AA.
AC Q8X8F1;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
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};
GN OrderedLocusNames=Z4658, ECs4153;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 -!- DOMAIN: Composed of an N- and a C-terminal domain. The N-terminal
CC domain carries the tetrahydrofolate (THF)-binding site and the C-
CC terminal domain is presumably involved in positioning the Met-tRNA
CC substrate for the formylation reaction.
CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000255|HAMAP-
CC Rule:MF_00182}.
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DR EMBL; AE005174; AAG58409.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37576.1; -; Genomic_DNA.
DR PIR; A91148; A91148.
DR PIR; E85993; E85993.
DR RefSeq; NP_312180.1; NC_002695.1.
DR RefSeq; WP_000004459.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X8F1; -.
DR SMR; Q8X8F1; -.
DR STRING; 155864.EDL933_4505; -.
DR EnsemblBacteria; AAG58409; AAG58409; Z4658.
DR EnsemblBacteria; BAB37576; BAB37576; ECs_4153.
DR GeneID; 915992; -.
DR KEGG; ece:Z4658; -.
DR KEGG; ecs:ECs_4153; -.
DR PATRIC; fig|386585.9.peg.4336; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_2_6; -.
DR OMA; CCPVVAY; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 Gene3D; 3.10.25.10; -; 1.
DR HAMAP; MF_00182; Formyl_trans; 1.
DR InterPro; IPR005794; Fmt.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR037022; Formyl_trans_C_sf.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR001555; GART_AS.
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.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
KW Protein biosynthesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..315
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_0000082961"
FT REGION 2..189
FT /note="N-terminal domain"
FT REGION 210..315
FT /note="C-terminal domain"
FT BINDING 113..116
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ SEQUENCE 315 AA; 34140 MW; BB369A5BAE498907 CRC64;
MSESLRIIFA GTPDFAARHL DALLSSGHNV VGVFTQPDRP AGRGKKLMPS PVKVLAEEKG
LPVFQPVSLR PQENQQLVAD LQADVMVVVA YGLILPKAVL EMPRLGCINV HGSLLPRWRG
AAPIQRSLWA GDAETGVTIM QMDVGLDTGD MLYKLSCPIT AEDTSGTLYD KLAELGPQGL
ITTLKQLADG TAKPEVQDET LVTYAEKLSK EEARIDWSLS AAQLERCIRA FNPWPMSWVE
IEGQPVKVWK ASVIDTATNA APGTILEANK QGIQVATGDG ILNLLSLQPA GKKAMSAQDL
LNSRREWFVP GNRLV