ID   TMCAL_LISW6             Reviewed;         392 AA.
AC   A0AKE9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=lwe2063;
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS   NCTC 11857 / SLCC 5334 / V8).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=386043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX   PubMed=16936040; DOI=10.1128/jb.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA   Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA   Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA   Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT   "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT   genome reduction with Listeria innocua as compared to Listeria
RT   monocytogenes.";
RL   J. Bacteriol. 188:7405-7415(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; AM263198; CAK21481.1; -; Genomic_DNA.
DR   RefSeq; WP_011702825.1; NC_008555.1.
DR   AlphaFoldDB; A0AKE9; -.
DR   SMR; A0AKE9; -.
DR   STRING; 386043.lwe2063; -.
DR   EnsemblBacteria; CAK21481; CAK21481; lwe2063.
DR   GeneID; 61189963; -.
DR   KEGG; lwe:lwe2063; -.
DR   eggNOG; COG1323; Bacteria.
DR   HOGENOM; CLU_038915_0_2_9; -.
DR   OMA; WARTKMA; -.
DR   OrthoDB; 1547014at2; -.
DR   Proteomes; UP000000779; 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..392
FT                   /note="tRNA(Met) cytidine acetate ligase"
FT                   /id="PRO_0000300181"
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         162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT   BINDING         187..188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
SQ   SEQUENCE   392 AA;  43823 MW;  39548121D0D0FE68 CRC64;
     MKATGIVVEY NPFHNGHQLH LNKARELTKA DVVIAVMSGS FVQRGEPAIL PKWERTKMAL
     AAGVDMVVEL PVSFATQHAT IFAEESVRIL DALHVDALFF GSEHGVSEDF LTAAKTVVEH
     EASFNQAIQL ALIDKKTSYA RAYTETFKQS FGTELLDVTK PNNILGFHYA LAIQKQNPTI
     SLQTMARIHA GYHDIEANHD QIASATAIRK LLLAGNLEEA SRYLPASSIE ILKNYDGPFL
     SWENYWALLK YRLIQAETDE LEGIRNVSEG IQNRMQIAAT KAQYFSDFIE SMKTKRYSNA
     RIQRTALQIL LNARNIPSAP YIRILGMNKT GQKYLSHHKK NISLPIVTTV SKAAPGLLEE
     DLRATNIYTL VKGLENYQAG DFHIPPILKS QT