ID   A0A2A9CST8_9ACTN        Unreviewed;       318 AA.
AC   A0A2A9CST8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=ATK74_2080 {ECO:0000313|EMBL:PFG17507.1};
OS   Propionicimonas paludicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Propionicimonas.
OX   NCBI_TaxID=185243 {ECO:0000313|EMBL:PFG17507.1, ECO:0000313|Proteomes:UP000226079};
RN   [1] {ECO:0000313|EMBL:PFG17507.1, ECO:0000313|Proteomes:UP000226079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15597 {ECO:0000313|EMBL:PFG17507.1,
RC   ECO:0000313|Proteomes:UP000226079};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2017) 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:PFG17507.1}.
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DR   EMBL; PDJC01000001; PFG17507.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9CST8; -.
DR   OrthoDB; 9800307at2; -.
DR   Proteomes; UP000226079; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
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; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF02367; TsaE; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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:UP000226079};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT   DOMAIN          17..171
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   318 AA;  33783 MW;  29A317ABF464E812 CRC64;
     MQRTLLAESL LGDGRALQIV TAEAWNAQVL SDVILDAFGN RPVIDPPPPA LAETPESVAS
     ALTDGFGVLA LVDDEPAGVV IVSFDGDASG IHRVSVRPVF QRLGIASAMI AVVLESLALR
     GVHRVGLVAR AEFPQVVAWW QRHGFVETSR QGTALQLTRE LPVCVMARTA EETQDLGHRL
     AGLLRAGDLI IAAGDLGAGK TTLTQGIGAG LNVAGAVISP TFVLSRVHRP LADGPALVHV
     DAYRLGSPAE LYDLDLDASA ADAVTLVEWG TGIAEGLADD RLEIDIRRSL DPEDETRWIF
     LTPIGERWTA VRPLLEAL
//