ID   TMCAL_LACP3             Reviewed;         378 AA.
AC   Q038B5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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}; OrderedLocusNames=LSEI_1684;
OS   Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS   CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 / NRRL
RC   B-441;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000423; ABJ70457.1; -; Genomic_DNA.
DR   RefSeq; WP_011674575.1; NC_008526.1.
DR   RefSeq; YP_806899.1; NC_008526.1.
DR   AlphaFoldDB; Q038B5; -.
DR   SMR; Q038B5; -.
DR   STRING; 321967.LSEI_1684; -.
DR   EnsemblBacteria; ABJ70457; ABJ70457; LSEI_1684.
DR   KEGG; lca:LSEI_1684; -.
DR   PATRIC; fig|321967.11.peg.1664; -.
DR   HOGENOM; CLU_038915_0_2_9; -.
DR   OMA; WARTKMA; -.
DR   Proteomes; UP000001651; 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..378
FT                   /note="tRNA(Met) cytidine acetate ligase"
FT                   /id="PRO_0000300172"
FT   BINDING         7..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT   BINDING         153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT   BINDING         178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
SQ   SEQUENCE   378 AA;  41698 MW;  45FE0AF04767585E CRC64;
     MQTVGMIAEF NPFHTGHAYA LAQARKLAQA DVVVVVMSGN YVQRGEPAIF DKWIRAQAAL
     QHGADIVVEL PVTGAVQAAD QFAEAGVTAL AAMGVNTLAF GTEHPEVAYA DLAEKLATAA
     LTGDGFRDYT QTYATQLNAV YAKAAGITQT DPNFMLGLSY AKANLALKRP MTLLPFARRG
     IGHDEVGIQA NIASASTVRE YLRADQSVEA IVPTELVDFY AKQQQYSWAQ FFPWLKYRLQ
     TAELNELRLV ATMAEGLEYR FTQKIDDAQD MTAFLKQVKS KRYTYARLRR LALAITLNMT
     ATAVNQARQH PQLHVLGFTP TGRQYLNSVK HDLDWPLLTK VSADMLAPDG VLAMTHRADR
     LITTIGGVEQ NYGRRPLM