ID   TRUB_SALPB              Reviewed;         314 AA.
AC   A9N730;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=SPAB_04096;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX69422.1; -; Genomic_DNA.
DR   RefSeq; WP_000089673.1; NC_010102.1.
DR   AlphaFoldDB; A9N730; -.
DR   SMR; A9N730; -.
DR   KEGG; spq:SPAB_04096; -.
DR   PATRIC; fig|1016998.12.peg.3859; -.
DR   HOGENOM; CLU_032087_0_3_6; -.
DR   OMA; ELQFIRW; -.
DR   BioCyc; SENT1016998:SPAB_RS16640-MON; -.
DR   Proteomes; UP000008556; 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   Gene3D; 2.30.130.10; -; 1.
DR   HAMAP; MF_01080; TruB_bact; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR002501; PsdUridine_synth_N.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR   InterPro; IPR015240; tRNA_sdUridine_synth_fam1_C.
DR   InterPro; IPR032819; TruB_C.
DR   PANTHER; PTHR13767; PTHR13767; 1.
DR   Pfam; PF09157; TruB-C_2; 1.
DR   Pfam; PF16198; TruB_C_2; 1.
DR   Pfam; PF01509; TruB_N; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00431; TruB; 1.
PE   3: Inferred from homology;
KW   Isomerase; tRNA processing.
FT   CHAIN           1..314
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_1000084667"
FT   ACT_SITE        48
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   314 AA;  35028 MW;  BD1E7BE85C9E90E4 CRC64;
     MSRPRRRGRD IHGVLLLDKP QGMSSNDVLQ KVKRIYNANR AGHTGALDPL ATGMLPICLG
     EATKFSQYLL DSDKRYRVIA RLGQRTDTSD ADGQIVQERP VTFSAEQLAS ALETFRGDIE
     QIPSMYSALK YQGKKLYEYA RQGIEVPREA RPITVYELLF IRHEGNELEL EVHCSKGTYI
     RTIIDDLGEK LGCGAHVTYL RRLTVSKYPV DRMVTLEHLQ TLVAQAEQQG VPAAQLLDPL
     LMPMDSPASD YPVVNLPLTS SVYFKNGNPV RTTGAPLKGL VRVTEGEDDK FIGMGEIDDE
     GRVAPRRLVV DYPA