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Database: UniProt
Entry: Q9PJ28
LinkDB: Q9PJ28
Original site: Q9PJ28 
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   14-MAY-2014, entry version 82.
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; ALYPRAF; -.
DR   OrthoDB; EOG6B09WV; -.
DR   BioCyc; CJEJ192222:GJTS-94-MONOMER; -.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
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; SSF50486; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   TIGRFAMs; TIGR00460; fmt; 1.
DR   PROSITE; PS00373; GART; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Protein biosynthesis; Reference proteome;
KW   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
//
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