ID   TRUB_BORAP              Reviewed;         282 AA.
AC   Q0SM48; G0IRY5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=BAPKO_0856, BafPKo_0831;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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; CP000395; ABH02080.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL70020.1; -; Genomic_DNA.
DR   RefSeq; WP_004789449.1; NC_017238.1.
DR   AlphaFoldDB; Q0SM48; -.
DR   SMR; Q0SM48; -.
DR   STRING; 390236.BafPKo_0831; -.
DR   EnsemblBacteria; AEL70020; AEL70020; BafPKo_0831.
DR   KEGG; baf:BAPKO_0856; -.
DR   KEGG; bafz:BafPKo_0831; -.
DR   PATRIC; fig|390236.22.peg.792; -.
DR   eggNOG; COG0130; Bacteria.
DR   HOGENOM; CLU_032087_0_2_12; -.
DR   OMA; ELQFIRW; -.
DR   OrthoDB; 1166299at2; -.
DR   Proteomes; UP000005216; 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   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   PANTHER; PTHR13767; PTHR13767; 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..282
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_1000084554"
FT   ACT_SITE        39
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   282 AA;  32065 MW;  878D47EFBE6155FA CRC64;
     MENGFLLINK EQGKTSFETL FPIKKYFNTN HVGHAGILDK FASGILIALV GKYTKLANYF
     MSLDKEYVAE FRFGLETDTL DPNGRIVNKT DYIPNLEDID LKLKDFVGEI YQSPPRFSSV
     HINGSRAYKL ALNGKFFEIK KRRVNVYDIQ RLSYDFSSSL LSLKISCSKG TYIRSIARDL
     AYSLNSCAYV SSLKRTKVGI FRLEDSTLCK NLSKASLISL ESLKSFEKVC IDSSKINLVK
     NGAYVEIQIN INEFKILKSR EGEILAVIKG IDLNKYKYVI IF