FMT_CHLPN
ID FMT_CHLPN Reviewed; 321 AA.
AC Q9Z7Q5; Q9JQG3; Q9K2D9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=CPn_0649, CP_0098, CpB0675;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) 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, ECO:0000305}.
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DR EMBL; AE001363; AAD18788.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF37982.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98856.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98604.1; -; Genomic_DNA.
DR PIR; B72051; B72051.
DR PIR; F81615; F81615.
DR PIR; F86571; F86571.
DR RefSeq; NP_224845.1; NC_000922.1.
DR RefSeq; WP_010883287.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z7Q5; -.
DR SMR; Q9Z7Q5; -.
DR STRING; 115711.CP_0098; -.
DR PRIDE; Q9Z7Q5; -.
DR EnsemblBacteria; AAD18788; AAD18788; CPn_0649.
DR EnsemblBacteria; AAF37982; AAF37982; CP_0098.
DR GeneID; 45050699; -.
DR KEGG; cpa:CP_0098; -.
DR KEGG; cpj:fmt; -.
DR KEGG; cpn:CPn_0649; -.
DR KEGG; cpt:CpB0675; -.
DR PATRIC; fig|115713.3.peg.719; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_1_0; -.
DR OrthoDB; 2009156at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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..321
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_0000082945"
FT BINDING 111..114
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
FT CONFLICT 279
FT /note="I -> V (in Ref. 2; AAF37982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 34540 MW; FCADE08CB30432DB CRC64;
MNLKVVYFGT PTFAATVLQD LLHHKIQITA VVTRVDKPQK RSAQLIPSPV KTIALTHGLP
LLQPSKASDP QFIEELRAFN ADVFIVVAYG AILRQIVLDI PRYGCYNLHA GLLPAYRGAA
PIQRCIMEGA TESGNTVIRM DAGMDTGDMA NITRVPIGPD MTSGELADAL ASQGAEVLIK
TLQQIESGQL QLVSQDAALA TIAPKLSKEE GQVPWDKPAK EAYAHIRGVT PAPGAWTLFS
FSEKAPKRLM IRKASLLAEA GRYGAPGTVV VTDRQELAIA CSEGAICLHE VQVEGKGSTN
SKSFLNGYPA KKLKIVFTLN N
