ID   TMCA_ACTP2              Reviewed;         596 AA.
AC   A3N059;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=tRNA(Met) cytidine acetyltransferase TmcA {ECO:0000255|HAMAP-Rule:MF_01886};
DE            EC=2.3.1.193 {ECO:0000255|HAMAP-Rule:MF_01886};
GN   Name=tmcA {ECO:0000255|HAMAP-Rule:MF_01886}; OrderedLocusNames=APL_0695;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
CC   -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at
CC       the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl
CC       donor and ATP (or GTP). {ECO:0000255|HAMAP-Rule:MF_01886}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O =
CC         ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) +
CC         phosphate; Xref=Rhea:RHEA:43788, Rhea:RHEA-COMP:10693, Rhea:RHEA-
CC         COMP:10694, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC         EC=2.3.1.193; Evidence={ECO:0000255|HAMAP-Rule:MF_01886};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01886}.
CC   -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. TmcA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01886}.
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DR   EMBL; CP000569; ABN73795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3N059; -.
DR   SMR; A3N059; -.
DR   STRING; 416269.APL_0695; -.
DR   EnsemblBacteria; ABN73795; ABN73795; APL_0695.
DR   KEGG; apl:APL_0695; -.
DR   eggNOG; COG1444; Bacteria.
DR   HOGENOM; CLU_004652_1_1_6; -.
DR   OMA; NEPDDLG; -.
DR   Proteomes; UP000001432; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051392; F:tRNA N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0002101; P:tRNA wobble cytosine modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.890; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01886; tRNA_acetyltr_TmcA; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR007807; Helicase_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032672; TmcA/NAT10/Kre33.
DR   InterPro; IPR038321; TmcA_C_sf.
DR   InterPro; IPR033442; TmcA_tRNA_bind.
DR   InterPro; IPR024914; tRNA_acetyltr_TmcA.
DR   PANTHER; PTHR10925; PTHR10925; 2.
DR   Pfam; PF13718; GNAT_acetyltr_2; 2.
DR   Pfam; PF05127; Helicase_RecD; 1.
DR   Pfam; PF17176; tRNA_bind_3; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ATP-binding; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..596
FT                   /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT                   /id="PRO_0000403117"
FT   DOMAIN          328..481
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         160..169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         285
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         406..408
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         413..419
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ   SEQUENCE   596 AA;  68436 MW;  D87F65FA4D63CC9A CRC64;
     MILAEMPPLD GGIVIHSGNI SQAKQYLGQE HPYAIYDMRA EGDVWLNLDA LAIIAGTIQA
     QGTLYLICPN WDTLEQQLDF DSQRWNGGKV IATPNFYRYF KALVQKFGFQ FQTLEETDFS
     LPKQPPQCQA TESLTPQQQK IFEKLPLDSS AIHLITAPRG RGKSTLAGKL AQQLAKTESV
     LITARSHSVL PSFWKSVAQH IPFFAPDHLL QKIAANQIAA KSWLFIDESA SLPLPMLHQF
     CEYFDKVVLT TTTHNYEGTG RGFSLKFPQQ LTKQYREWRL TKPLRWHEND PLEQFIDELL
     IMSPPSETNQ YAEFYHLLAE AHYKTTPSDL RRLFDAQDQL LHSFSEHQRL VGGIWAVPEG
     DLEPELAEAI WRGERRPQGN LVAQYLCFQG NLLEACQLRS VRISRIAVQP ELQKQGIGKR
     LISDFILQKI QQTRPLVDYV SVSFGLSEPL LHFWQQCGFQ LVQITPTKEA SSGYHSAMML
     YPISAEGQRF VQQATARFER DLALQPFYAE LQNMLPIRPL VQLQMDEQDW RNIEGFALAQ
     RSLAASYVSL TRLYRQDPRN HGVLANLWQQ FERIQGKKEW LENLRSLLAN YLQYTR