ID   TSAD_STAA8              Reviewed;         341 AA.
AC   Q2FWL2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   04-NOV-2026, entry version 120.
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01445};
DE            EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_01445};
DE            Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445};
GN   Name=tsaD {ECO:0000255|HAMAP-Rule:MF_01445}; Synonyms=gcp;
GN   OrderedLocusNames=SAOUHSC_02277;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION IN CELL VIABILITY.
RX   PubMed=15837383; DOI=10.1016/j.femsle.2005.03.017;
RA   Zheng L., Yang J., Landwehr C., Fan F., Ji Y.;
RT   "Identification of an essential glycoprotease in Staphylococcus aureus.";
RL   FEMS Microbiol. Lett. 245:279-285(2005).
RN   [3]
RP   FUNCTION.
RX   PubMed=17237169; DOI=10.1128/jb.01806-06;
RA   Zheng L., Yu C., Bayles K., Lasa I., Ji Y.;
RT   "Conditional mutation of an essential putative glycoprotease eliminates
RT   autolysis in Staphylococcus aureus.";
RL   J. Bacteriol. 189:2734-2742(2007).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC       adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC       with adenine. Is involved in the transfer of the threonylcarbamoyl
CC       moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC       together with TsaE and TsaB. TsaD likely plays a direct catalytic role
CC       in this reaction (By similarity). Critical mediator involved in the
CC       modification of cell wall peptidoglycan synthesis and/or cell division
CC       as well as in the positive regulation of the activities of different
CC       murein hydrolases. Essential for cell viability. Negatively affects the
CC       expression of lrgA. Positively affects cidA expression, maybe
CC       indirectly. May be an important chelator of excess zinc. Down-
CC       regulation of gcp/tsaD eliminates penicillin- and vancomycin-caused
CC       cell lysis, inhibits several extracellular hydrolase activities,
CC       dramatically increasing tolerance to hydrolases and leads to a
CC       bacteriostatic effect. {ECO:0000255|HAMAP-Rule:MF_01445,
CC       ECO:0000269|PubMed:15837383, ECO:0000269|PubMed:17237169}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonylcarbamoyladenylate + adenosine(37) in tRNA = N(6)-L-
CC         threonylcarbamoyladenosine(37) in tRNA + AMP + H(+);
CC         Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01445};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01445};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01445};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01445}.
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DR   EMBL; CP000253; ABD31315.1; -; Genomic_DNA.
DR   RefSeq; WP_000159034.1; NC_007795.1.
DR   RefSeq; YP_500758.1; NC_007795.1.
DR   AlphaFoldDB; Q2FWL2; -.
DR   SMR; Q2FWL2; -.
DR   STRING; 93061.SAOUHSC_02277; -.
DR   PaxDb; 93061-SAOUHSC_02277; -.
DR   GeneID; 3919152; -.
DR   KEGG; sao:SAOUHSC_02277; -.
DR   PATRIC; fig|93061.5.peg.2067; -.
DR   eggNOG; COG0533; Bacteria.
DR   HOGENOM; CLU_023208_0_2_9; -.
DR   OMA; AAAHEIY; -.
DR   OrthoDB; 9806197at2; -.
DR   PRO; PR:Q2FWL2; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061711; F:tRNA N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR   CDD; cd24133; ASKHA_NBD_TsaD_bac; 1.
DR   FunFam; 3.30.420.40:FF:000012; tRNA N6-adenosine threonylcarbamoyltransferase; 1.
DR   FunFam; 3.30.420.40:FF:000040; tRNA N6-adenosine threonylcarbamoyltransferase; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_01445; TsaD; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   InterPro; IPR017860; Peptidase_M22_CS.
DR   InterPro; IPR022450; TsaD.
DR   NCBIfam; TIGR00329; gcp_kae1; 1.
DR   NCBIfam; TIGR03723; T6A_TsaD_YgjD; 1.
DR   PANTHER; PTHR11735; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR11735:SF6; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00814; TsaD; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS01016; GLYCOPROTEASE; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Iron; Metal-binding; Reference proteome;
KW   Transferase; tRNA processing.
FT   CHAIN           1..341
FT                   /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT                   /id="PRO_0000303551"
FT   BINDING         115
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         119
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         137..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         304
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
SQ   SEQUENCE   341 AA;  36819 MW;  AB4C57F8D21132C6 CRC64;
     MTKDILILAV ETSCDETSVS VIKNGRDILS NTVLSQIESH KRFGGVVPEV ASRHHVEGIT
     ATINEALGDA DVSIEDIDAI AVTEGPGLIG ALLIGVNAAK ALAFAYDKPL IPVHHIAGHI
     YANHIEEPLT FPLIALIVSG GHTELVYMKD HLSFEVIGET RDDAVGEAYD KVARTIGLNY
     PGGPQVDRLA AEGEDTYSFP RVWLDKDSYD FSFSGLKSAV INQLHNQRQK NIPIIEANVA
     TSFQNSVVEV LTFKAIQACK EYGVQRLIVA GGVASNKGLR QSLADQCKVN DIQLTIPSPK
     LCTDNAAMIG VAGHYLYQQG RFADLALNGH SNIDLEEYSA E
//