FMT_YERPE
ID FMT_YERPE Reviewed; 315 AA.
AC Q8ZJ80; Q0WK66;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=YPO0241, y4022, YP_0239;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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; AL590842; CAL18924.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM87566.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS60515.1; -; Genomic_DNA.
DR PIR; AB0030; AB0030.
DR RefSeq; WP_002209020.1; NZ_WHLN01000072.1.
DR RefSeq; YP_002345322.1; NC_003143.1.
DR PDB; 3R8X; X-ray; 2.26 A; A=1-315.
DR PDBsum; 3R8X; -.
DR AlphaFoldDB; Q8ZJ80; -.
DR SMR; Q8ZJ80; -.
DR STRING; 214092.YPO0241; -.
DR PaxDb; Q8ZJ80; -.
DR DNASU; 1148969; -.
DR EnsemblBacteria; AAM87566; AAM87566; y4022.
DR EnsemblBacteria; AAS60515; AAS60515; YP_0239.
DR GeneID; 66843910; -.
DR KEGG; ype:YPO0241; -.
DR KEGG; ypk:y4022; -.
DR KEGG; ypm:YP_0239; -.
DR PATRIC; fig|214092.21.peg.469; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_2_6; -.
DR OMA; CCPVVAY; -.
DR EvolutionaryTrace; Q8ZJ80; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IBA:GO_Central.
DR GO; GO:0071951; P:conversion of methionyl-tRNA to N-formyl-methionyl-tRNA; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Protein biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..315
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_0000083093"
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"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:3R8X"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:3R8X"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:3R8X"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3R8X"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:3R8X"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3R8X"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:3R8X"
FT HELIX 165..188
FT /evidence="ECO:0007829|PDB:3R8X"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3R8X"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:3R8X"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:3R8X"
FT TURN 231..235
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 244..254
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:3R8X"
FT STRAND 278..289
FT /evidence="ECO:0007829|PDB:3R8X"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:3R8X"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:3R8X"
SQ SEQUENCE 315 AA; 34140 MW; 24F167229DC2E0C8 CRC64;
MSDSLRIIFA GTPDFAARHL GALLSSQHKI VGVFTQPDRP AGRGNKLTPS PVKILAEHHG
IPVFQPKSLR PEENQHLVAD LNADIMVVVA YGLILPAAVL AMPRLGCINV HGSLLPRWRG
AAPIQRSVWA GDEKTGITIM QMDIGLDTGA MLHKIECAIQ PEDTSATLYD KLAQLGPQGL
LITLQQLAAG TALAEVQNET QATYAEKLSK EEAKLDWTLS ATQLERCIRA FNPWPVSYFI
VDEQPIKVWQ AQVLPAGEDA EPGTIIHADK HGIQVATADG VLNITQLQPA GKKAMSAADL
LNSRREWFIP GSQLV
