ID   TRHP1_BACSU             Reviewed;         422 AA.
AC   O32034;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=tRNA hydroxylation protein P1 {ECO:0000303|PubMed:31253794};
DE            EC=3.4.-.- {ECO:0000305};
GN   Name=trhP1 {ECO:0000303|PubMed:31253794}; Synonyms=yrrO;
GN   OrderedLocusNames=BSU27340;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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-methoxyuridine (mo5U) biosynthesis.
CC       {ECO:0000269|PubMed:31253794}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant lacking both trhP1 and trhP2
CC       shows reduced 5-methoxyuridine (mo5U) formation in tRNAs.
CC       {ECO:0000269|PubMed:31253794}.
CC   -!- SIMILARITY: Belongs to the peptidase U32 family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB14676.1; -; Genomic_DNA.
DR   PIR; H69979; H69979.
DR   RefSeq; NP_390612.1; NC_000964.3.
DR   RefSeq; WP_003229802.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O32034; -.
DR   IntAct; O32034; 1.
DR   STRING; 224308.BSU27340; -.
DR   MEROPS; U32.002; -.
DR   jPOST; O32034; -.
DR   PaxDb; O32034; -.
DR   PRIDE; O32034; -.
DR   EnsemblBacteria; CAB14676; CAB14676; BSU_27340.
DR   GeneID; 937561; -.
DR   KEGG; bsu:BSU27340; -.
DR   PATRIC; fig|224308.179.peg.2970; -.
DR   eggNOG; COG0826; Bacteria.
DR   InParanoid; O32034; -.
DR   OMA; YGGVSHF; -.
DR   PhylomeDB; O32034; -.
DR   BioCyc; BSUB:BSU27340-MON; -.
DR   Proteomes; UP000001570; Chromosome.
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; IMP:UniProtKB.
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   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; tRNA processing.
FT   CHAIN           1..422
FT                   /note="tRNA hydroxylation protein P1"
FT                   /id="PRO_0000360803"
SQ   SEQUENCE   422 AA;  47629 MW;  7B937F9F2A215AB6 CRC64;
     MTAVNDKIST IVNGKRVITK KPELLAPAGN LEKLKIAVHY GADAVFIGGQ EYGLRSNADN
     FTIEEIAEGV EFAKKYGAKI YVTTNIFAHN ENMDGLEDYL KALGDANVAG IIVADPLIIE
     TCRRVAPNVE VHLSTQQSLS NWKAVQFWKE EGLDRVVLAR ETSALEIREM KEKVDIEIES
     FIHGAMCIAY SGRCVLSNHM TARDSNRGGC CQSCRWDYDL YQTDGANAVA LYGEEDAPFA
     MSPKDLKLIE SIPKMIEMGI DSLKIEGRMK SIHYVATVVS VYRKVIDAYC ADPENFVIQK
     EWLEELDKCA NRDTATAFFE GTPGYEEQMF GEHAKKTTYD FVGLVLNYDE DTQMVTLQQR
     NFFKKGDEVE FFGPEIENFT HTIETIWDED GNELDAARHP LQIVKFKLDK KIYPSNMMRK
     GK