TSAD_STAA8
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 03-AUG-2022, entry version 106.
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; Firmicutes; Bacilli; Bacillales; 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=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
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;
CC Evidence={ECO:0000255|HAMAP-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; NZ_LS483365.1.
DR RefSeq; YP_500758.1; NC_007795.1.
DR AlphaFoldDB; Q2FWL2; -.
DR SMR; Q2FWL2; -.
DR STRING; 1280.SAXN108_2292; -.
DR EnsemblBacteria; ABD31315; ABD31315; 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; HLEGHIY; -.
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:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF6; PTHR11735:SF6; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1.
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
