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Database: UniProt
Entry: A0A0F7HKR0_9STAP
LinkDB: A0A0F7HKR0_9STAP
Original site: A0A0F7HKR0_9STAP 
ID   A0A0F7HKR0_9STAP        Unreviewed;       314 AA.
AC   A0A0F7HKR0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|ARBA:ARBA00012261, ECO:0000256|HAMAP-Rule:MF_00182};
DE            EC=2.1.2.9 {ECO:0000256|ARBA:ARBA00012261, ECO:0000256|HAMAP-Rule:MF_00182};
GN   Name=fmt {ECO:0000256|HAMAP-Rule:MF_00182};
GN   ORFNames=AAT16_05585 {ECO:0000313|EMBL:AKG73736.1}, SAMN05216235_0357
GN   {ECO:0000313|EMBL:SFK55064.1};
OS   Salinicoccus halodurans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Salinicoccus.
OX   NCBI_TaxID=407035 {ECO:0000313|EMBL:AKG73736.1, ECO:0000313|Proteomes:UP000034029};
RN   [1] {ECO:0000313|EMBL:AKG73736.1, ECO:0000313|Proteomes:UP000034029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3B36 {ECO:0000313|EMBL:AKG73736.1,
RC   ECO:0000313|Proteomes:UP000034029};
RX   PubMed=26634017;
RA   Jiang K., Xue Y., Ma Y.;
RT   "Complete genome sequence of Salinicoccus halodurans H3B36, isolated from
RT   the Qaidam Basin in China.";
RL   Stand. Genomic Sci. 10:116-116(2015).
RN   [2] {ECO:0000313|Proteomes:UP000034029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3B36 {ECO:0000313|Proteomes:UP000034029};
RA   Ma Y., Jiang K., Xue Y.;
RT   "Complete genome sequence of Salinicoccus halodurans strain H3B36, isolated
RT   from the Qaidam basin of China.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SFK55064.1, ECO:0000313|Proteomes:UP000183090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6501 {ECO:0000313|EMBL:SFK55064.1,
RC   ECO:0000313|Proteomes:UP000183090};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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:0000256|HAMAP-Rule:MF_00182}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-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:78530,
CC         ChEBI:CHEBI:78844, ChEBI:CHEBI:195366; EC=2.1.2.9;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00182};
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000256|ARBA:ARBA00010699,
CC       ECO:0000256|HAMAP-Rule:MF_00182}.
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DR   EMBL; CP011366; AKG73736.1; -; Genomic_DNA.
DR   EMBL; FOTB01000001; SFK55064.1; -; Genomic_DNA.
DR   RefSeq; WP_046789924.1; NZ_FOTB01000001.1.
DR   AlphaFoldDB; A0A0F7HKR0; -.
DR   STRING; 407035.AAT16_05585; -.
DR   KEGG; shv:AAT16_05585; -.
DR   PATRIC; fig|407035.3.peg.1163; -.
DR   OrthoDB; 9802815at2; -.
DR   Proteomes; UP000034029; Chromosome.
DR   Proteomes; UP000183090; Unassembled WGS sequence.
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; 3.40.50.12230; -; 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   NCBIfam; TIGR00460; fmt; 1.
DR   PANTHER; PTHR11138; METHIONYL-TRNA FORMYLTRANSFERASE; 1.
DR   PANTHER; PTHR11138:SF5; METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   PROSITE; PS00373; GART; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00182};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00182}.
FT   DOMAIN          4..180
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   DOMAIN          204..302
FT                   /note="Formyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02911"
FT   BINDING         110..113
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   314 AA;  33807 MW;  948FBE74AE1244E2 CRC64;
     MNEKIIFMGT PDFSVPVLKA LHEKHPVSMV ISQPDKPVGR KRVMTPPPVA AAAEEMGIPL
     FQPDRIREEA AVEKIKELDP DLIITAAYGQ ILPKALLEIP RLGAVNVHAS LLPRHRGGAP
     IHRAILEGDS ETGISIMYMA EGLDSGDVIS RSATGIMDDD NTGTLHDRLS AIGSELLLET
     LPSILDGTNT RTPQDAERVT VSPNISKEDE LLDWTRDARD VFNHIRGLSP WPGAYTSFDG
     KRLKIYGAKL PEGKSDAEPG VITDVTESGF TVACGDGNTV EVTEVQLSGK KKTDAQNFAA
     GRQGLTGTVM GQVD
//
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