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Database: UniProt
Entry: A0A0Q4V8B2_9MICO
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ID   A0A0Q4V8B2_9MICO        Unreviewed;       168 AA.
AC   A0A0Q4V8B2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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   ORFNames=ASF23_04955 {ECO:0000313|EMBL:KQO63584.1};
OS   Curtobacterium sp. Leaf261.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO63584.1, ECO:0000313|Proteomes:UP000050821};
RN   [1] {ECO:0000313|EMBL:KQO63584.1, ECO:0000313|Proteomes:UP000050821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf261 {ECO:0000313|EMBL:KQO63584.1,
RC   ECO:0000313|Proteomes:UP000050821};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQO63584.1, ECO:0000313|Proteomes:UP000050821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf261 {ECO:0000313|EMBL:KQO63584.1,
RC   ECO:0000313|Proteomes:UP000050821};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQO63584.1}.
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DR   EMBL; LMMJ01000007; KQO63584.1; -; Genomic_DNA.
DR   RefSeq; WP_055950815.1; NZ_LMMJ01000007.1.
DR   AlphaFoldDB; A0A0Q4V8B2; -.
DR   STRING; 1736311.ASF23_04955; -.
DR   OrthoDB; 9800307at2; -.
DR   Proteomes; UP000050821; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050821}.
FT   REGION          130..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   168 AA;  17506 MW;  37998F35F29781B2 CRC64;
     MTLLLDERVD GTAAMGELGA RLAAVLRAGD LVVLTGPLGA GKTTMTRGLG AALGARGQVS
     SPTFVLARTH PTAAGPDLVH VDAYRLSDPV ELDDLDLDWD GAIVVVEWGR GMVDGVSENV
     LDVEISRATG ADADSDVDDP DLDPDDVPDE PRRVVVTGIG PRWEGIAI
//
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