ID E3D9S5_GARV3 Unreviewed; 189 AA.
AC E3D9S5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaE {ECO:0000256|ARBA:ARBA00019010};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE {ECO:0000256|ARBA:ARBA00032441};
GN OrderedLocusNames=HMPREF0421_20737 {ECO:0000313|EMBL:ADP38819.1};
OS Gardnerella vaginalis (strain ATCC 14019 / 317).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP38819.1, ECO:0000313|Proteomes:UP000001453};
RN [1] {ECO:0000313|EMBL:ADP38819.1, ECO:0000313|Proteomes:UP000001453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA Wilson B.A.;
RT "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT differences in metabolic and virulence potential.";
RL PLoS ONE 5:E12411-E12411(2010).
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 TsaD and TsaB. TsaE seems to play an indirect role in the
CC t(6)A biosynthesis pathway, possibly in regulating the core enzymatic
CC function of TsaD. {ECO:0000256|ARBA:ARBA00024908}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TsaE family.
CC {ECO:0000256|ARBA:ARBA00007599}.
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DR EMBL; CP002104; ADP38819.1; -; Genomic_DNA.
DR RefSeq; YP_003985842.1; NC_014644.1.
DR AlphaFoldDB; E3D9S5; -.
DR KEGG; gvg:HMPREF0421_20737; -.
DR PATRIC; fig|525284.18.peg.730; -.
DR HOGENOM; CLU_087829_1_1_11; -.
DR OMA; SVIVVEW; -.
DR OrthoDB; 9800307at2; -.
DR Proteomes; UP000001453; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003442; T6A_TsaE.
DR NCBIfam; TIGR00150; T6A_YjeE; 1.
DR PANTHER; PTHR33540; TRNA THREONYLCARBAMOYLADENOSINE BIOSYNTHESIS PROTEIN TSAE; 1.
DR PANTHER; PTHR33540:SF2; TRNA THREONYLCARBAMOYLADENOSINE BIOSYNTHESIS PROTEIN TSAE; 1.
DR Pfam; PF02367; TsaE; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|EMBL:ADP38819.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ SEQUENCE 189 AA; 20494 MW; 4958A09FE46B6D60 CRC64;
MILENHNIKK LVIPTGSCMR DLGKTIAKIV HETDVILLSG PLGAGKTTFA QGFGQGLGIK
DPIVSPTFTI ARELKGTFSD GKVANLIHVD AYRLGGKDYA PGQDTVSRLL DELESLGLDE
ALEEPGEGTV VLMEWGEQMA GVLADVRLEI HIDRPIDKEK SNEFTSEGKR VVTLVPVGGD
WCDRLKILD
//