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FMT_BACAN
ID   FMT_BACAN               Reviewed;         314 AA.
AC   Q81WH2; Q6HUM0; Q6KNV4;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=BA_4004, GBAA_4004, BAS3717;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE016879; AAP27732.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT33120.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT56019.1; -; Genomic_DNA.
DR   RefSeq; NP_846246.1; NC_003997.3.
DR   RefSeq; WP_000598790.1; NZ_WXXJ01000026.1.
DR   RefSeq; YP_029968.1; NC_005945.1.
DR   PDB; 4IQF; X-ray; 2.40 A; A/B/C/D=1-314.
DR   PDBsum; 4IQF; -.
DR   AlphaFoldDB; Q81WH2; -.
DR   SMR; Q81WH2; -.
DR   STRING; 260799.BAS3717; -.
DR   DNASU; 1086742; -.
DR   EnsemblBacteria; AAP27732; AAP27732; BA_4004.
DR   EnsemblBacteria; AAT33120; AAT33120; GBAA_4004.
DR   GeneID; 45023695; -.
DR   KEGG; ban:BA_4004; -.
DR   KEGG; bar:GBAA_4004; -.
DR   KEGG; bat:BAS3717; -.
DR   PATRIC; fig|198094.11.peg.3974; -.
DR   eggNOG; COG0223; Bacteria.
DR   HOGENOM; CLU_033347_1_1_9; -.
DR   OMA; CCPVVAY; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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   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..314
FT                   /note="Methionyl-tRNA formyltransferase"
FT                   /id="PRO_0000082910"
FT   BINDING         110..113
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   HELIX           13..22
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   STRAND          26..31
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   TURN            39..42
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   HELIX           48..55
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   HELIX           69..78
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   STRAND          81..87
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   HELIX           94..97
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   STRAND          104..110
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   STRAND          114..118
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   HELIX           120..126
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   HELIX           162..185
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   HELIX           196..198
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   HELIX           207..210
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   HELIX           218..226
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   TURN            227..232
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   STRAND          234..238
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   STRAND          241..252
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   STRAND          261..265
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   STRAND          270..272
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   STRAND          275..287
FT                   /evidence="ECO:0007829|PDB:4IQF"
FT   HELIX           295..301
FT                   /evidence="ECO:0007829|PDB:4IQF"
SQ   SEQUENCE   314 AA;  34736 MW;  8E81D02492DABEE2 CRC64;
     MIKVVFMGTP DFSVPVLRRL IEDGYDVIGV VTQPDRPVGR KKVLTPTPVK VEAEKHGIPV
     LQPLRIREKD EYEKVLALEP DLIVTAAFGQ IVPNEILEAP KYGCINVHAS LLPELRGGAP
     IHYAIMEGKE KTGITIMYMV EKLDAGDILT QVEVEIEERE TTGSLFDKLS EAGAHLLSKT
     VPLLIQGKLE PIKQNEEEVT FAYNIKREQE KIDWTKTGEE VYNHIRGLNP WPVAYTTLAG
     QVVKVWWGEK VPVTKSAEAG TIVAIEEDGF VVATGNETGV KITELQPSGK KRMSCSQFLR
     GTKPEIGTKL GENA
 
 
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