FMT_BART1
ID FMT_BART1 Reviewed; 309 AA.
AC A9ILK1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=BT_0078;
OS Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=382640;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 105476 / IBS 506;
RX PubMed=18037886; DOI=10.1038/ng.2007.38;
RA Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT "Genomic analysis of Bartonella identifies type IV secretion systems as
RT host adaptability factors.";
RL Nat. Genet. 39:1469-1476(2007).
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; AM260525; CAK00574.1; -; Genomic_DNA.
DR RefSeq; WP_012230390.1; NC_010161.1.
DR AlphaFoldDB; A9ILK1; -.
DR SMR; A9ILK1; -.
DR STRING; 382640.BT_0078; -.
DR EnsemblBacteria; CAK00574; CAK00574; BT_0078.
DR KEGG; btr:BT_0078; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_2_5; -.
DR OMA; CCPVVAY; -.
DR OrthoDB; 2009156at2; -.
DR Proteomes; UP000001592; 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; 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; Transferase.
FT CHAIN 1..309
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_1000077288"
FT BINDING 112..115
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ SEQUENCE 309 AA; 33789 MW; ADEEEFEEA0868A2D CRC64;
MALRLSFMGT PDFSVPILHA LLDAGHDVVA VYSQPPRPAG RRRLKLIPSP VQNAAEERSI
PTFTPQTLKT AEQQAQFAAL SVDAAIVVAY GLLLPKAILE TPRFGCFNAH ASLLPRWRGA
APIQRAIMAG DKETGMMIMK MDEGLDTGSI VLSRSIPITD TTTTDKLSNE LSYIGAELMI
ETLSTLEKGQ LKLIPQSKEG ITYAAKIKKE ETRIDWKKPA EFIHRHIRAL SPSPGCWCNM
NIGGREERVK ILESRLATGT SLEIGRIEPN SLIVHCGQGR IEITTLQRSG GKILDSATFL
RGAHISAVF
