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Database: UniProt/SWISS-PROT
Entry: FMT_GEOSL
LinkDB: FMT_GEOSL
Original site: FMT_GEOSL 
ID   FMT_GEOSL               Reviewed;         317 AA.
AC   Q74GW4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   19-FEB-2014, entry version 63.
DE   RecName: Full=Methionyl-tRNA formyltransferase;
DE            EC=2.1.2.9;
GN   Name=fmt; OrderedLocusNames=GSU0130;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R.,
RA   Van Aken S.E., Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR33465.1; -; Genomic_DNA.
DR   RefSeq; NP_951192.1; NC_002939.5.
DR   ProteinModelPortal; Q74GW4; -.
DR   STRING; 243231.GSU0130; -.
DR   EnsemblBacteria; AAR33465; AAR33465; GSU0130.
DR   GeneID; 2687945; -.
DR   KEGG; gsu:GSU0130; -.
DR   PATRIC; 22023008; VBIGeoSul17553_0131.
DR   eggNOG; COG0223; -.
DR   HOGENOM; HOG000261177; -.
DR   KO; K00604; -.
DR   OMA; KVWKAEV; -.
DR   OrthoDB; EOG6B09WV; -.
DR   ProtClustDB; CLSK827657; -.
DR   BioCyc; GSUL243231:GH27-136-MONOMER; -.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-HAMAP.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Protein biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN         1    317       Methionyl-tRNA formyltransferase.
FT                                /FTId=PRO_0000082969.
FT   REGION      112    115       Tetrahydrofolate (THF) binding (By
FT                                similarity).
SQ   SEQUENCE   317 AA;  34668 MW;  BAF582625EF358A2 CRC64;
     MAGLRIIFMG TPEFACPTLR KLIERGEEVI AVVTQPDRPK GRGQKLVPPP VKALAQEHDI
     PVLQPLKVRT PESVDEIRRL APDLIVVVAF GQILPQSLLD IPKHGCINIH ASLLPRYRGA
     APLNWCLING ETETGITTMM MDAGLDTGDM LVKRAIPIGP DEDAQSLHDR LSQLGAETID
     ETLDLLLAGK LVREKQDDSL TCYAPMLKKE DGLVDWTREP VQVKNQVRGF TPWPGAYTFL
     DGKTLKLYRV AVAGETGEPG EILRVGREGI LVGCGSGSIL IQELQLEGRK RLPTAEFLAG
     FRLEPGTRLG EAGSVEH
//
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