ID   TRUB_STRPB              Reviewed;         294 AA.
AC   Q1JBI5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=tRNA pseudouridine synthase B {ECO:0000255|HAMAP-Rule:MF_01080};
DE            EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE            Short=Psi55 synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA pseudouridylate synthase {ECO:0000255|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA-uridine isomerase {ECO:0000255|HAMAP-Rule:MF_01080};
GN   Name=truB {ECO:0000255|HAMAP-Rule:MF_01080};
GN   OrderedLocusNames=MGAS2096_Spy1021;
OS   Streptococcus pyogenes serotype M12 (strain MGAS2096).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370553;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS2096;
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA   Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in the
RT   human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in
CC       the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01080}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC         Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01080};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01080}.
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DR   EMBL; CP000261; ABF36073.1; -; Genomic_DNA.
DR   RefSeq; WP_002989678.1; NC_008023.1.
DR   AlphaFoldDB; Q1JBI5; -.
DR   SMR; Q1JBI5; -.
DR   KEGG; spj:MGAS2096_Spy1021; -.
DR   HOGENOM; CLU_032087_0_1_9; -.
DR   OMA; ELQFIRW; -.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR   CDD; cd02573; PseudoU_synth_EcTruB; 1.
DR   HAMAP; MF_01080; TruB_bact; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR002501; PsdUridine_synth_N.
DR   InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR   InterPro; IPR032819; TruB_C.
DR   PANTHER; PTHR13767; PTHR13767; 1.
DR   Pfam; PF16198; TruB_C_2; 1.
DR   Pfam; PF01509; TruB_N; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00431; TruB; 1.
PE   3: Inferred from homology;
KW   Isomerase; tRNA processing.
FT   CHAIN           1..294
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_1000084697"
FT   ACT_SITE        39
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   294 AA;  32345 MW;  9129B3E6AB9FD758 CRC64;
     MINGIINLKK EAGMTSHDAV FKLRKLLQEK KIGHGGTLDP DVVGVLPIAV GKATRVIEYM
     TEAGKVYEGQ VTLGYSTTTE DASGEVVARS SLPAVLTEEL VDQTMTTFLG KITQTPPMYS
     AVKVNGRKLY EYARAGESVE RPRREVTISL FERTSPLNFT EDGLCRFSFK VACSKGTYVR
     TLAVDLGRAL GVESHMSFLQ RSASAGLTLE TAYTLGEIAD MVSKQEMSFL LPIEYGVADL
     PKMVIDDTEL TEISFGRRLS LPSQEPLLAA FHGEKVIAIL EKRDQEYKPK KVLI