ID   TMCAL_STAS1             Reviewed;         377 AA.
AC   Q49WQ0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=SSP1662;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18807.1; -; Genomic_DNA.
DR   RefSeq; WP_011303392.1; NZ_MTGA01000039.1.
DR   AlphaFoldDB; Q49WQ0; -.
DR   SMR; Q49WQ0; -.
DR   STRING; 342451.SSP1662; -.
DR   EnsemblBacteria; BAE18807; BAE18807; SSP1662.
DR   KEGG; ssp:SSP1662; -.
DR   PATRIC; fig|342451.11.peg.1661; -.
DR   eggNOG; COG1323; Bacteria.
DR   HOGENOM; CLU_038915_0_2_9; -.
DR   OMA; WARTKMA; -.
DR   OrthoDB; 1547014at2; -.
DR   Proteomes; UP000006371; 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; Reference proteome;
KW   RNA-binding; tRNA processing; tRNA-binding.
FT   CHAIN           1..377
FT                   /note="tRNA(Met) cytidine acetate ligase"
FT                   /id="PRO_0000300191"
FT   BINDING         7..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT   BINDING         100
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   377 AA;  42863 MW;  EEE78E162EE64988 CRC64;
     MKSVALVTEY NPFHNGHLYH AQQSKSITNS DISIAIMSGN FVMRGQPAIY NKFTRAKMAL
     RAVDLVVELP AYASVSAGQY FAKTAVQIAD YLNVSHLSFG SESGNMDDFL SLAQSIDKIE
     QSPLFLEKLK EGKSYPRILS ELITDNDLLS SPNNTLGLSY VRAIQTYAPS IQPWTISRFQ
     SAHHDNEISH QTFASGTSIR QSLMNQTDLW KDVVPCEIHK HYERPHISIE DTFNYLKYAI
     LSQDATSLAQ IYTMSEGIEN RILQTIEQAT SFEHLMTLLK TKRYTYTHIQ RLLMNILLNF
     KKHDEPASIN AVRILGMSER GQQYLKQIKK SFPERNFVTQ VNKQNANLFT NEIHATKIYN
     LISGQTANDF NTPVIRI