ID   TRHP2_BACSU             Reviewed;         309 AA.
AC   O32035;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=tRNA hydroxylation protein P2 {ECO:0000303|PubMed:31253794};
DE            EC=3.4.-.- {ECO:0000305};
GN   Name=trhP2 {ECO:0000303|PubMed:31253794}; Synonyms=yrrN;
GN   OrderedLocusNames=BSU27350;
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; CAB14677.1; -; Genomic_DNA.
DR   PIR; G69979; G69979.
DR   RefSeq; NP_390613.1; NC_000964.3.
DR   RefSeq; WP_004399094.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O32035; -.
DR   SMR; O32035; -.
DR   STRING; 224308.BSU27350; -.
DR   MEROPS; U32.A02; -.
DR   jPOST; O32035; -.
DR   PaxDb; O32035; -.
DR   PRIDE; O32035; -.
DR   EnsemblBacteria; CAB14677; CAB14677; BSU_27350.
DR   GeneID; 937559; -.
DR   KEGG; bsu:BSU27350; -.
DR   PATRIC; fig|224308.179.peg.2971; -.
DR   eggNOG; COG0826; Bacteria.
DR   InParanoid; O32035; -.
DR   OMA; TCNYWGR; -.
DR   PhylomeDB; O32035; -.
DR   BioCyc; BSUB:BSU27350-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   Pfam; PF01136; Peptidase_U32; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; tRNA processing.
FT   CHAIN           1..309
FT                   /note="tRNA hydroxylation protein P2"
FT                   /id="PRO_0000360789"
SQ   SEQUENCE   309 AA;  35079 MW;  BF33AA8018227BCE CRC64;
     MKKPELLVTP TSTADILPLI QAGATAFLVG EQRYGLRLAG EFSREDVTKA VEIAHKEGAK
     VYVAVNAIFH NDKVGELGEY LAFLAEAGVD AAVFGDPAVL MAARESAPDL KLHWSTETTG
     TNYYTCNYWG RKGAARSVLA RELNMDSIVE IKENAEVEIE IQVHGMTCMF QSKRSLIGNY
     FEYQGKVMDI ERKKKESGMF LHDKERDNKY PIFEDENGTH IMSPNDVCII DELEELIDAG
     IDSFKIDGVL KMPEYLIEVT KMYREAIDLC VENRDEYEAK KEDWIERIES IQPVNRKIDT
     GFFFKETVY