ID   TRUB_BARBK              Reviewed;         320 AA.
AC   A1UU52;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=BARBAKC583_1256;
OS   Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=360095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA   Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA   Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA   Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA   Fraser-Ligget C., Seshadri R.;
RL   Submitted (DEC-2006) 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; CP000524; ABM45296.1; -; Genomic_DNA.
DR   RefSeq; WP_005767988.1; NC_008783.1.
DR   AlphaFoldDB; A1UU52; -.
DR   SMR; A1UU52; -.
DR   STRING; 360095.BARBAKC583_1256; -.
DR   EnsemblBacteria; ABM45296; ABM45296; BARBAKC583_1256.
DR   KEGG; bbk:BARBAKC583_1256; -.
DR   PATRIC; fig|360095.6.peg.1232; -.
DR   eggNOG; COG0130; Bacteria.
DR   HOGENOM; CLU_032087_0_3_5; -.
DR   OMA; ELQFIRW; -.
DR   OrthoDB; 1166299at2; -.
DR   Proteomes; UP000000643; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..320
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_1000084551"
FT   ACT_SITE        49
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   320 AA;  35474 MW;  E22AC6C3AEE143D0 CRC64;
     MSRQSKKKGR SISGWVILDK PKAMKSTEAV SKIKRLFNAQ KAGHAGTLDP LASGLLPIAL
     GEATKTVPYV MEGTKTYHFH VAWGEERSTD DLEGVVTKTS SKRPTQEEIF ALLPKYTGVI
     LQTPPQFSAI KIAGNRAYDL AREGEIFEIP PRQVKIDSLE LIGTTDQGYS IFEMTCGKGT
     YVRSLARDMG HDLGCYGYIA DLRRTAVAPF CENDLITWDA LKAAIPHENT TDENCIPLKQ
     NFSTLDGLLI ETDVALKCLA HYTLNQIQAQ RVRMGNSILL CDQNMPTSNI DICVTYKAQL
     LAIGTIDQNQ FKPKRIFTTL