TRUB_STRPC
ID TRUB_STRPC Reviewed; 294 AA.
AC Q1JLG7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=MGAS9429_Spy1065;
OS Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370551;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS9429;
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; CP000259; ABF32252.1; -; Genomic_DNA.
DR RefSeq; WP_002989678.1; NC_008021.1.
DR AlphaFoldDB; Q1JLG7; -.
DR SMR; Q1JLG7; -.
DR EnsemblBacteria; ABF32252; ABF32252; MGAS9429_Spy1065.
DR GeneID; 57852717; -.
DR KEGG; spk:MGAS9429_Spy1065; -.
DR HOGENOM; CLU_032087_0_1_9; -.
DR OMA; ELQFIRW; -.
DR Proteomes; UP000002433; Chromosome.
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_1000084698"
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