ID   TRHP_HELPJ              Reviewed;         422 AA.
AC   Q9ZMR3;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=tRNA hydroxylation protein P {ECO:0000250|UniProtKB:P76403};
DE            EC=3.4.-.- {ECO:0000305};
DE   Flags: Precursor;
GN   Name=trhP {ECO:0000250|UniProtKB:P76403}; OrderedLocusNames=jhp_0155;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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.
CC       {ECO:0000250|UniProtKB:P76403}.
CC   -!- SIMILARITY: Belongs to the peptidase U32 family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD05738.1; -; Genomic_DNA.
DR   PIR; D71966; D71966.
DR   RefSeq; WP_001077418.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZMR3; -.
DR   STRING; 85963.jhp_0155; -.
DR   MEROPS; U32.002; -.
DR   EnsemblBacteria; AAD05738; AAD05738; jhp_0155.
DR   KEGG; hpj:jhp_0155; -.
DR   PATRIC; fig|85963.30.peg.867; -.
DR   eggNOG; COG0826; Bacteria.
DR   OMA; YGGVSHF; -.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR001539; Peptidase_U32.
DR   Pfam; PF01136; Peptidase_U32; 1.
DR   PROSITE; PS01276; PEPTIDASE_U32; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Signal; tRNA processing.
FT   SIGNAL          1..58
FT                   /evidence="ECO:0000255"
FT   CHAIN           59..422
FT                   /note="tRNA hydroxylation protein P"
FT                   /id="PRO_0000028527"
SQ   SEQUENCE   422 AA;  47259 MW;  B68EE4900937CBD8 CRC64;
     MNQVELLSPA GNLKKLKIAL NYGADAVYGG VSHFSLRNRA GKEFTLETFK EGIDYAHALD
     KKVYATINGF PFNSQLKLLE EHLYKMAELE PDAFIIAAPG VIKLASKIAP HIPVHLSTQA
     NVLNTLDAQV FYDLGVKRIV CARELSLNDA VEIKKALPDL ELEIFVHGSM CFAFSGRCLI
     SALQKGRVPN RGSCANDCRF DYEYYVKNPD NGVMMRLVEE EGVGTHIFNA KDLNLSGHIA
     EILSSNAISA LKIEGRTKSS YYAAQTTRIY RLAVDDFYHN TLKPSFYASE LNTLKNRGFT
     DGYLMRRPFE RLDTQNHQTA ISEGDFQVNG EITEDGRFFA CKFTTTTNTA YEIIAPKNAA
     ITPIVNDIGK IYTFEKRSYL VLYKILLENN TELETIHSGN VNLVRLPAPL PAFSFLRTQV
     RV