TRHP_ECOLI
ID TRHP_ECOLI Reviewed; 453 AA.
AC P76403; O08007; O08010;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=tRNA hydroxylation protein P {ECO:0000303|PubMed:31253794};
DE EC=3.4.-.- {ECO:0000305};
GN Name=trhP {ECO:0000303|PubMed:31253794}; Synonyms=yegQ;
GN OrderedLocusNames=b2081, JW2066;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-162; HIS-166;
RP CYS-170; CYS-177; CYS-193 AND CYS-197.
RX PubMed=31253794; DOI=10.1038/s41467-019-10750-8;
RA Sakai Y., Kimura S., Suzuki T.;
RT "Dual pathways of tRNA hydroxylation ensure efficient translation by
RT expanding decoding capability.";
RL Nat. Commun. 10:2858-2858(2019).
CC -!- FUNCTION: Involved in prephenate-dependent formation of 5-
CC hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first
CC step in 5-carboxymethoxyuridine (cmo5U) biosynthesis (PubMed:31253794).
CC Involved differently in ho5U formation in each tRNA; tRNA(Leu3) and
CC tRNA(Pro3) are major targets of TrhP (PubMed:31253794).
CC {ECO:0000269|PubMed:31253794}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant cells display reduced 5-
CC methoxycarbonylmethoxyuridine (mcmo5U) formation in tRNA(Ala1),
CC tRNA(Ser1) and tRNA(Thr4) (PubMed:31253794). Reduced 5-
CC carboxymethoxyuridine (cmo5U) formation in tRNA(Val1)
CC (PubMed:31253794). Strongly reduced cmo5U formation in tRNA(Leu3) and
CC tRNA(Pro3) (PubMed:31253794). Cells lacking both trhP and trhO show
CC complete absence of 5-carboxymethoxyuridine (cmo5U) modification in
CC tRNAs; cells display a temperature-sensitive phenotype and decode
CC codons ending in G (GCG and UCG) less efficiently than the wild-type
CC strain (PubMed:31253794). {ECO:0000269|PubMed:31253794}.
CC -!- SIMILARITY: Belongs to the peptidase U32 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC75142.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15936.1; -; Genomic_DNA.
DR PIR; H64974; H64974.
DR RefSeq; NP_416585.1; NC_000913.3.
DR RefSeq; WP_000476011.1; NZ_STEB01000002.1.
DR AlphaFoldDB; P76403; -.
DR SMR; P76403; -.
DR BioGRID; 4263508; 43.
DR DIP; DIP-11887N; -.
DR IntAct; P76403; 8.
DR STRING; 511145.b2081; -.
DR MEROPS; U32.002; -.
DR jPOST; P76403; -.
DR PaxDb; P76403; -.
DR PRIDE; P76403; -.
DR EnsemblBacteria; AAC75142; AAC75142; b2081.
DR EnsemblBacteria; BAA15936; BAA15936; BAA15936.
DR GeneID; 66674017; -.
DR GeneID; 946609; -.
DR KEGG; ecj:JW2066; -.
DR KEGG; eco:b2081; -.
DR PATRIC; fig|511145.12.peg.2159; -.
DR EchoBASE; EB3813; -.
DR eggNOG; COG0826; Bacteria.
DR HOGENOM; CLU_011540_0_2_6; -.
DR InParanoid; P76403; -.
DR OMA; YGGVSHF; -.
DR PhylomeDB; P76403; -.
DR BioCyc; EcoCyc:G7118-MON; -.
DR PRO; PR:P76403; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:EcoCyc.
DR InterPro; IPR001539; Peptidase_U32.
DR InterPro; IPR032525; Peptidase_U32_C.
DR Pfam; PF01136; Peptidase_U32; 1.
DR Pfam; PF16325; Peptidase_U32_C; 1.
DR PROSITE; PS01276; PEPTIDASE_U32; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; tRNA processing.
FT CHAIN 1..453
FT /note="tRNA hydroxylation protein P"
FT /id="PRO_0000079184"
FT MUTAGEN 162
FT /note="E->A: Reduced 5-carboxymethoxyuridine formation in
FT tRNAs."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 166
FT /note="H->A: Reduced 5-carboxymethoxyuridine formation in
FT tRNAs."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 170
FT /note="C->A: Reduced 5-carboxymethoxyuridine formation in
FT tRNAs."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 177
FT /note="C->A: Reduced 5-carboxymethoxyuridine formation in
FT tRNAs."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 193
FT /note="C->A: Reduced 5-carboxymethoxyuridine formation in
FT tRNAs."
FT /evidence="ECO:0000269|PubMed:31253794"
FT MUTAGEN 197
FT /note="C->A: Reduced 5-carboxymethoxyuridine formation in
FT tRNAs."
FT /evidence="ECO:0000269|PubMed:31253794"
SQ SEQUENCE 453 AA; 51193 MW; 1843AB6D040ECDDF CRC64;
MFKPELLSPA GTLKNMRYAF AYGADAVYAG QPRYSLRVRN NEFNHENLQL GINEAHALGK
KFYVVVNIAP HNAKLKTFIR DLKPVVEMGP DALIMSDPGL IMLVREHFPE MPIHLSVQAN
AVNWATVKFW QQMGLTRVIL SRELSLEEIE EIRNQVPDME IEIFVHGALC MAYSGRCLLS
GYINKRDPNQ GTCTNACRWE YNVQEGKEDD VGNIVHKYEP IPVQNVEPTL GIGAPTDKVF
MIEEAQRPGE YMTAFEDEHG TYIMNSKDLR AIAHVERLTK MGVHSLKIEG RTKSFYYCAR
TAQVYRKAID DAAAGKPFDT SLLETLEGLA HRGYTEGFLR RHTHDDYQNY EYGYSVSDRQ
QFVGEFTGER KGDLAAVAVK NKFSVGDSLE LMTPQGNINF TLEHMENAKG EAMPIAPGDG
YTVWLPVPQD LELNYALLMR NFSGETTRNP HGK
