ID   TRUB_LACLM              Reviewed;         330 AA.
AC   A2RL47;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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}; OrderedLocusNames=llmg_1431;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL98013.1; -; Genomic_DNA.
DR   RefSeq; WP_011835288.1; NZ_WJVF01000011.1.
DR   AlphaFoldDB; A2RL47; -.
DR   SMR; A2RL47; -.
DR   STRING; 416870.llmg_1431; -.
DR   EnsemblBacteria; CAL98013; CAL98013; llmg_1431.
DR   KEGG; llm:llmg_1431; -.
DR   eggNOG; COG0130; Bacteria.
DR   HOGENOM; CLU_032087_0_1_9; -.
DR   OMA; ELQFIRW; -.
DR   PhylomeDB; A2RL47; -.
DR   BioCyc; LLAC416870:LLMG_RS07220-MON; -.
DR   Proteomes; UP000000364; 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..330
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_1000084614"
FT   ACT_SITE        42
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   330 AA;  36561 MW;  FD19C0B96FA99212 CRC64;
     MNENLNGILN VYKEAGWTSF DVVAKLRGIL KTKKIGHGGT LDPSVTGVLP IAVGKSTRLL
     EYMEAAGKIY EGQVTIGFST ETEDADGAIV NQTPVKNNLT ESEIDSAMSH FVGKIKQIPP
     MYSAVKINGK KLYEYARAGQ TIERPAREIT IKSFVRTSPI DWNKEEGLVT FSFKVECSKG
     TYVRTLAVDL ADSLGYAGHM SKLQRTASNG LLIKDAIKLS KIEEIKESGK LSTILYPAEY
     AVSDLPRVNL TTVQFDMARV GKKFAQSDWT NEVETADSSV NKTKQQEYLL TDLSLLTTEK
     FAAFYNDKLV AVYMKHPEKE GIWKPNKVLV