ID FMT_CAMJE Reviewed; 305 AA.
AC Q9PJ28; Q0PC39;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 01-MAY-2013, entry version 75.
DE RecName: Full=Methionyl-tRNA formyltransferase;
DE EC=2.1.2.9;
GN Name=fmt; OrderedLocusNames=Cj0098;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W.,
RA Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
RA Whitehead S., Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- FUNCTION: Modifies the free amino group of the aminoacyl moiety of
CC methionyl-tRNA(fMet). The formyl group appears to play a dual role
CC in the initiator identity of N-formylmethionyl-tRNA by: (I)
CC promoting its recognition by IF2 and (II) impairing its binding to
CC EFTu-GTP (By similarity).
CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl-
CC tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).
CC -!- SIMILARITY: Belongs to the fmt family.
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DR EMBL; AL111168; CAL34269.1; -; Genomic_DNA.
DR PIR; B81426; B81426.
DR RefSeq; YP_002343558.1; NC_002163.1.
DR ProteinModelPortal; Q9PJ28; -.
DR STRING; 192222.Cj0098; -.
DR EnsemblBacteria; CAL34269; CAL34269; Cj0098.
DR GeneID; 904427; -.
DR KEGG; cje:Cj0098; -.
DR PATRIC; 20057123; VBICamJej33762_0096.
DR eggNOG; COG0223; -.
DR HOGENOM; HOG000261177; -.
DR KO; K00604; -.
DR OMA; FDKITPK; -.
DR ProtClustDB; PRK00005; -.
DR BioCyc; CJEJ192222:GJTS-94-MONOMER; -.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:HAMAP.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006413; P:translational initiation; IEA:GOC.
DR Gene3D; 3.10.25.10; -; 1.
DR Gene3D; 3.40.50.170; -; 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; IPR011034; Formyl_transferase_C-like.
DR InterPro; IPR001555; GART_AS.
DR InterPro; IPR015518; Met_tRNA_Form_TA-like.
DR PANTHER; PTHR11138; PTHR11138; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF50486; FMT_C_like; 1.
DR SUPFAM; SSF53328; formyl_transf; 1.
DR TIGRFAMs; TIGR00460; fmt; 1.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
KW Complete proteome; Methyltransferase; Protein biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1 305 Methionyl-tRNA formyltransferase.
FT /FTId=PRO_0000082938.
FT REGION 111 114 Tetrahydrofolate (THF) binding (By
FT similarity).
SQ SEQUENCE 305 AA; 34069 MW; 770DE65901EE5009 CRC64;
MKKIIFMGTP SYATCILKAL VENENFKLVA LFTQPDKAVG RKQILTPSDT KAFLSQNYPS
IPIFTPSSLK DKNIIREIKD LNPDFIVVAA YGKILPKAIL DLAPCVNLHA SLLPKYRGAS
PIQSAILNKD EKSGVCTMLM EEGLDTGAIL ESLECDIKDK NSSEVFELLA NLAAKIILST
LLNFDKITPK KQEESLATLC RKIKKEDGLI NLQNARELYQ KYLAFTPWPG VFLENGLKFL
ELELVDELKQ NAKMGEILEL EKESFLLACK QGVLRIKKLQ ESGKKALDGR TYLNGKRLKS
EDSLC
//
