ID   TMCAL_STRPC             Reviewed;         368 AA.
AC   Q1JNE5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=tRNA(Met) cytidine acetate ligase {ECO:0000255|HAMAP-Rule:MF_01539};
DE            EC=6.3.4.- {ECO:0000255|HAMAP-Rule:MF_01539};
GN   Name=tmcAL {ECO:0000255|HAMAP-Rule:MF_01539};
GN   OrderedLocusNames=MGAS9429_Spy0266;
OS   Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS9429;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
CC   -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at
CC       the wobble position of elongator tRNA(Met), using acetate and ATP as
CC       substrates. First activates an acetate ion to form acetyladenylate (Ac-
CC       AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
CC       {ECO:0000255|HAMAP-Rule:MF_01539}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP +
CC         diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met);
CC         Xref=Rhea:RHEA:58144, Rhea:RHEA-COMP:10693, Rhea:RHEA-COMP:10694,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01539};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01539}.
CC   -!- SIMILARITY: Belongs to the TmcAL family. {ECO:0000255|HAMAP-
CC       Rule:MF_01539}.
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DR   EMBL; CP000259; ABF31454.1; -; Genomic_DNA.
DR   RefSeq; WP_002991082.1; NC_008021.1.
DR   AlphaFoldDB; Q1JNE5; -.
DR   SMR; Q1JNE5; -.
DR   EnsemblBacteria; ABF31454; ABF31454; MGAS9429_Spy0266.
DR   GeneID; 57852099; -.
DR   KEGG; spk:MGAS9429_Spy0266; -.
DR   HOGENOM; CLU_038915_0_2_9; -.
DR   OMA; WARTKMA; -.
DR   Proteomes; UP000002433; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01539; TmcAL; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR008513; tRNA(Met)_cyd_acetate_ligase.
DR   PANTHER; PTHR37825; PTHR37825; 1.
DR   Pfam; PF05636; HIGH_NTase1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; RNA-binding;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..368
FT                   /note="tRNA(Met) cytidine acetate ligase"
FT                   /id="PRO_0000300195"
FT   BINDING         7..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT   BINDING         96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT   BINDING         152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT   BINDING         175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
SQ   SEQUENCE   368 AA;  41646 MW;  FD28F2838027347E CRC64;
     MTVTGIIAEF NPFHNGHKYL LETAEGLKII AMSGNFMQRG EPALIDKWIR SEMALKNGAD
     IVVELPFFVS VQSADYFAQG AIDILCQLGI QQLAFGTENV IDYQKLIKVY EKKSEQMTAY
     LSTLEDTLSY PQKTQKMWEI FAGVKFSGQT PNHILGLSYA KASAGKHIQL CPIKRQGAAY
     HSKDKNHLLA SASAIRQHLN DWDFISHSVP NAGLLINNPH MSWDHYFSFL KYQILNHSDL
     TSIFQVNDEL ASRIKKAIKV SQNIDHLVDT VATKRYTKAR VRRILTYILV NAKEPTLPKG
     IHILGFTSKG QAHLKKLKKS RPLITRIGAE TWDEMTQKAD SIYQLGHQDI PEQSFGRIPI
     IIKNERLN