TAPT_ECOLI
ID TAPT_ECOLI Reviewed; 232 AA.
AC Q47319; Q2MAF3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=tRNA-uridine aminocarboxypropyltransferase {ECO:0000305};
DE EC=2.5.1.25 {ECO:0000269|PubMed:31804502, ECO:0000269|PubMed:31863583, ECO:0000269|PubMed:4597321};
DE AltName: Full=SAM-dependent 3-amino-3-carboxypropyl transferase {ECO:0000303|PubMed:31863583};
DE AltName: Full=tRNA U47 acp transferase A {ECO:0000303|PubMed:31863583};
DE AltName: Full=tRNA aminocarboxypropyltransferase {ECO:0000303|PubMed:31804502};
GN Name=tapT {ECO:0000303|PubMed:31804502};
GN Synonyms=tuaA {ECO:0000303|PubMed:31863583}, yfiP;
GN OrderedLocusNames=b2583, JW5409;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=4597321; DOI=10.1016/0006-291x(74)90603-2;
RA Nishimura S., Taya Y., Kuchino Y., Oashi Z.;
RT "Enzymatic synthesis of 3-(3-amino-3-carboxypropyl)uridine in Escherichia
RT coli phenylalanine transfer RNA: transfer of the 3-amino-acid-3-
RT carboxypropyl group from S-adenosylmethionine.";
RL Biochem. Biophys. Res. Commun. 57:702-708(1974).
RN [5]
RP IDENTIFICATION OF THE TDD SUPERFAMILY.
RX PubMed=25566315; DOI=10.3389/fgene.2014.00424;
RA Burroughs A.M., Aravind L.;
RT "Analysis of two domains with novel RNA-processing activities throws light
RT on the complex evolution of ribosomal RNA biogenesis.";
RL Front. Genet. 5:424-424(2014).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=31804502; DOI=10.1038/s41467-019-13525-3;
RA Takakura M., Ishiguro K., Akichika S., Miyauchi K., Suzuki T.;
RT "Biogenesis and functions of aminocarboxypropyluridine in tRNA.";
RL Nat. Commun. 10:5542-5542(2019).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, DOMAIN,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 1-MET--PRO-20; CYS-31; CYS-34;
RP CYS-41; CYS-43; ASP-137 AND TRP-140.
RC STRAIN=BW25993;
RX PubMed=31863583; DOI=10.1093/nar/gkz1191;
RA Meyer B., Immer C., Kaiser S., Sharma S., Yang J., Watzinger P., Weiss L.,
RA Kotter A., Helm M., Seitz H.M., Koetter P., Kellner S., Entian K.D.,
RA Woehnert J.;
RT "Identification of the 3-amino-3-carboxypropyl (acp) transferase enzyme
RT responsible for acp3U formation at position 47 in Escherichia coli tRNAs.";
RL Nucleic Acids Res. 48:1435-1450(2020).
CC -!- FUNCTION: Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine
CC (acp3U) at position 47 of tRNAs (PubMed:31804502, PubMed:31863583,
CC PubMed:4597321). Acp3U47 confers thermal stability on tRNA
CC (PubMed:31804502). {ECO:0000269|PubMed:31804502,
CC ECO:0000269|PubMed:31863583, ECO:0000269|PubMed:4597321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in tRNA + S-adenosyl-L-methionine = a 3-[(3S)-3-
CC amino-3-carboxypropyl]uridine in tRNA + H(+) + S-methyl-5'-
CC thioadenosine; Xref=Rhea:RHEA:62432, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC COMP:16092, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:82930; EC=2.5.1.25;
CC Evidence={ECO:0000269|PubMed:31804502, ECO:0000269|PubMed:31863583,
CC ECO:0000269|PubMed:4597321};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62433;
CC Evidence={ECO:0000269|PubMed:31804502, ECO:0000269|PubMed:31863583,
CC ECO:0000269|PubMed:4597321};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(47) in tRNA(Phe) = 3-[(3S)-
CC 3-amino-3-carboxypropyl]uridine(47) in tRNA(Phe) + H(+) + S-methyl-
CC 5'-thioadenosine; Xref=Rhea:RHEA:12300, Rhea:RHEA-COMP:10427,
CC Rhea:RHEA-COMP:10428, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:65315, ChEBI:CHEBI:82930; EC=2.5.1.25;
CC Evidence={ECO:0000269|PubMed:4597321};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12301;
CC Evidence={ECO:0000269|PubMed:4597321};
CC -!- ACTIVITY REGULATION: The degree of the acp3U modification at U47 is
CC dependent on the presence of the m7G modification at the preceding
CC nucleotide G46. It also depends on medium conditions.
CC {ECO:0000269|PubMed:31863583}.
CC -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:31863583}.
CC -!- DOMAIN: Contains 1 DXTW motif (PubMed:31863583). The N-terminal domain
CC binds zinc and is important for activity (PubMed:31863583).
CC {ECO:0000269|PubMed:31863583, ECO:0000305|PubMed:31863583}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to the loss of the
CC acp3U modification (PubMed:31804502, PubMed:31863583). Mutant has no
CC obvious defect under normal growth conditions (PubMed:31863583). It
CC shows motility defect and genome instability under continuous heat
CC stress (PubMed:31804502). {ECO:0000269|PubMed:31804502,
CC ECO:0000269|PubMed:31863583}.
CC -!- SIMILARITY: Belongs to the TDD superfamily. DTWD2 family. TapT
CC subfamily. {ECO:0000305|PubMed:25566315, ECO:0000305|PubMed:31804502}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA10924.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D64044; BAA10924.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75636.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76753.1; -; Genomic_DNA.
DR PIR; F65036; F65036.
DR RefSeq; NP_417078.4; NC_000913.3.
DR RefSeq; WP_001300438.1; NZ_LN832404.1.
DR AlphaFoldDB; Q47319; -.
DR BioGRID; 4261901; 5.
DR BioGRID; 851395; 1.
DR DIP; DIP-12067N; -.
DR IntAct; Q47319; 2.
DR STRING; 511145.b2583; -.
DR PaxDb; Q47319; -.
DR PRIDE; Q47319; -.
DR EnsemblBacteria; AAC75636; AAC75636; b2583.
DR EnsemblBacteria; BAE76753; BAE76753; BAE76753.
DR GeneID; 947057; -.
DR KEGG; ecj:JW5409; -.
DR KEGG; eco:b2583; -.
DR PATRIC; fig|511145.12.peg.2686; -.
DR EchoBASE; EB3975; -.
DR eggNOG; COG3148; Bacteria.
DR HOGENOM; CLU_066458_1_0_6; -.
DR InParanoid; Q47319; -.
DR OMA; WQPYVVF; -.
DR PhylomeDB; Q47319; -.
DR BioCyc; EcoCyc:G7349-MON; -.
DR BioCyc; MetaCyc:G7349-MON; -.
DR PRO; PR:Q47319; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016432; F:tRNA-uridine aminocarboxypropyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR InterPro; IPR005636; DTW.
DR InterPro; IPR039262; DTWD2/YfiP.
DR PANTHER; PTHR21392; PTHR21392; 1.
DR Pfam; PF03942; DTW; 1.
DR SMART; SM01144; DTW; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW tRNA processing; Zinc.
FT CHAIN 1..232
FT /note="tRNA-uridine aminocarboxypropyltransferase"
FT /id="PRO_0000169271"
FT MOTIF 137..140
FT /note="DXTW"
FT /evidence="ECO:0000305"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:31863583"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:31863583"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:31863583"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:31863583"
FT MUTAGEN 1..20
FT /note="Missing: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:31863583"
FT MUTAGEN 31
FT /note="C->S: Complete loss of activity; when associated
FT with S-34."
FT /evidence="ECO:0000269|PubMed:31863583"
FT MUTAGEN 34
FT /note="C->S: Complete loss of activity; when associated
FT with S-31."
FT /evidence="ECO:0000269|PubMed:31863583"
FT MUTAGEN 41
FT /note="C->S: Shows weak residual activity; when associated
FT with S-43."
FT /evidence="ECO:0000269|PubMed:31863583"
FT MUTAGEN 43
FT /note="C->S: Shows weak residual activity; when associated
FT with S-41."
FT /evidence="ECO:0000269|PubMed:31863583"
FT MUTAGEN 137
FT /note="D->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:31863583"
FT MUTAGEN 140
FT /note="W->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:31863583"
SQ SEQUENCE 232 AA; 25995 MW; C54CDA8CF563050B CRC64;
MTENAVLQLR AERIARATRP FLARGNRVRR CQRCLLPEKL CLCSTITPAQ AKSRFCLLMF
DTEPMKPSNT GRLIADILPD TVAFQWSRTE PSQDLLELVQ NPDYQPMVVF PASYADEQRE
VIFTPPAGKP PLFIMLDGTW PEARKMFRKS PYLDNLPVIS VDLSRLSAYR LREAQAEGQY
CTAEVAIALL DMAGDTGAAA GLGEHFTRFK TRYLAGKTQH LGSITAEQLE SV
