TMCAL_LIGS1
ID TMCAL_LIGS1 Reviewed; 380 AA.
AC Q1WUM1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=LSL_0505;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000233; ABD99314.1; -; Genomic_DNA.
DR RefSeq; WP_011475793.1; NC_007929.1.
DR RefSeq; YP_535397.1; NC_007929.1.
DR AlphaFoldDB; Q1WUM1; -.
DR SMR; Q1WUM1; -.
DR STRING; 362948.LSL_0505; -.
DR EnsemblBacteria; ABD99314; ABD99314; LSL_0505.
DR GeneID; 57058995; -.
DR KEGG; lsl:LSL_0505; -.
DR PATRIC; fig|362948.14.peg.583; -.
DR HOGENOM; CLU_038915_0_2_9; -.
DR OMA; WARTKMA; -.
DR Proteomes; UP000006559; 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:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR004821; Cyt_trans-like.
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.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome;
KW RNA-binding; tRNA processing; tRNA-binding.
FT CHAIN 1..380
FT /note="tRNA(Met) cytidine acetate ligase"
FT /id="PRO_0000300177"
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 151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
SQ SEQUENCE 380 AA; 43381 MW; 7A8C6AEA8567DFDD CRC64;
MKIIGIIAEY NPFHNGHLYQ IEKVKEIYPE SIIIVAMSGN FLQRGEPAIV DKWVRAKQAL
LNGVDVVVEI PIAGCVQPAD RFAENGVRIL NNMGCEELFF GAEHAEYDFM TYAQLVQNLD
STEFSKKNIS YAEAFQEAVA AKIGHNIDSP NDVLGLAYAK ANLKFGKKLK LNPISRNVAG
YHDKSLSPDS NIASATAIRK VLFSKDHNLV DKYLPSYQDL KDEKYISWDD FWPFLRYKLI
SSDIDELANI YGMAEGIQYR MKKKALELKV EATFDEWLKA VKSKRFTYTR LTRLSVATLV
GMKVNDVSLY NKFPYVHLLG FTKNGQKALN IMKKNSEIPL LAKISQQDKD DFYHVDYRAG
KIYQSQNYKE QDLKRAPLIF