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Database: UniProt
Entry: A0A075R539_BRELA
LinkDB: A0A075R539_BRELA
Original site: A0A075R539_BRELA 
ID   A0A075R539_BRELA        Unreviewed;       410 AA.
AC   A0A075R539;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=tRNA(Met) cytidine acetate ligase {ECO:0000256|HAMAP-Rule:MF_01539};
DE            EC=6.3.4.- {ECO:0000256|HAMAP-Rule:MF_01539};
GN   Name=tmcAL {ECO:0000256|HAMAP-Rule:MF_01539};
GN   ORFNames=BRLA_c033500 {ECO:0000313|EMBL:AIG27662.1};
OS   Brevibacillus laterosporus LMG 15441.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG27662.1, ECO:0000313|Proteomes:UP000005850};
RN   [1] {ECO:0000313|EMBL:AIG27662.1, ECO:0000313|Proteomes:UP000005850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG27662.1,
RC   ECO:0000313|Proteomes:UP000005850};
RX   PubMed=21914864; DOI=10.1128/JB.05696-11;
RA   Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT   "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT   invertebrates.";
RL   J. Bacteriol. 193:5535-5536(2011).
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:0000256|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:0000256|HAMAP-Rule:MF_01539};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01539}.
CC   -!- SIMILARITY: Belongs to the TmcAL family. {ECO:0000256|HAMAP-
CC       Rule:MF_01539}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01539}.
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DR   EMBL; CP007806; AIG27662.1; -; Genomic_DNA.
DR   RefSeq; WP_003336858.1; NZ_CP007806.1.
DR   AlphaFoldDB; A0A075R539; -.
DR   STRING; 1042163.BRLA_c033500; -.
DR   KEGG; blr:BRLA_c033500; -.
DR   eggNOG; COG1323; Bacteria.
DR   HOGENOM; CLU_038915_0_1_9; -.
DR   Proteomes; UP000005850; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; HUPs; 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; TRNA(MET) CYTIDINE ACETATE LIGASE; 1.
DR   PANTHER; PTHR37825:SF1; TRNA(MET) CYTIDINE ACETATE LIGASE; 1.
DR   Pfam; PF05636; HIGH_NTase1; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01539};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01539};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005850};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW   Transferase {ECO:0000313|EMBL:AIG27662.1};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01539}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01539}.
FT   BINDING         7..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT   BINDING         102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT   BINDING         165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT   BINDING         190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
SQ   SEQUENCE   410 AA;  45957 MW;  19C75F3D78D41251 CRC64;
     MKSVGLIVEY NPLHNGHKLH FALAKKMTGA DACVAVMSGN FLQRGEPAIV SKWARTEMAL
     RLGVDLVIEL PTVFATSNAE LFAHGAVSLL DRIGVVDTLC FGSECGDISW MKQAAQLLAH
     EAPEFSHLLK AGLRDGLPYP KAYAEAAHTY LTDHGIHGAA LDQPNNILGF NYLLSLARLN
     SKIVPVTIQR QKAGYHQETI TDEQIASATA LRKILTEQQQ KIAAVAGYVP RATVEVLQRE
     WLSGLYPMTW ENFAHPLFHR LLQLTAQELA TYHEIEEGME YRLLESVRRS KTVAQMISSA
     KSKRYTQNRI QRMLLNVLLD VKKDQISAFN LRHGASYARV LGFSQKGRAL LQQAKQKSAI
     PLYTNVRDGL HPMLDVDIRS NALYRLAHST QIEQPFLEEY RRIPLQITPE
//
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