ID B2IPR9_STRPS Unreviewed; 292 AA.
AC B2IPR9;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=tRNA pseudouridine synthase B {ECO:0000256|HAMAP-Rule:MF_01080};
DE EC=5.4.99.25 {ECO:0000256|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE Short=Psi55 synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA pseudouridylate synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA-uridine isomerase {ECO:0000256|HAMAP-Rule:MF_01080};
GN Name=truB {ECO:0000256|HAMAP-Rule:MF_01080,
GN ECO:0000313|EMBL:ACB90341.1};
GN OrderedLocusNames=SPCG_1089 {ECO:0000313|EMBL:ACB90341.1};
OS Streptococcus pneumoniae (strain CGSP14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=516950 {ECO:0000313|EMBL:ACB90341.1, ECO:0000313|Proteomes:UP000001682};
RN [1] {ECO:0000313|EMBL:ACB90341.1, ECO:0000313|Proteomes:UP000001682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGSP14 {ECO:0000313|EMBL:ACB90341.1,
RC ECO:0000313|Proteomes:UP000001682};
RX PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT "Genome evolution driven by host adaptations results in a more virulent and
RT antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL BMC Genomics 10:158-158(2009).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in
CC the psi GC loop of transfer RNAs. {ECO:0000256|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:0000256|ARBA:ARBA00000385, ECO:0000256|HAMAP-
CC Rule:MF_01080};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00005642, ECO:0000256|HAMAP-
CC Rule:MF_01080}.
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DR EMBL; CP001033; ACB90341.1; -; Genomic_DNA.
DR RefSeq; WP_001013245.1; NC_010582.1.
DR AlphaFoldDB; B2IPR9; -.
DR KEGG; spw:SPCG_1089; -.
DR HOGENOM; CLU_032087_0_1_9; -.
DR Proteomes; UP000001682; 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; 3.30.2350.10; Pseudouridine synthase; 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 NCBIfam; TIGR00431; TruB; 1.
DR PANTHER; PTHR13767:SF2; PSEUDOURIDYLATE SYNTHASE TRUB1; 1.
DR PANTHER; PTHR13767; TRNA-PSEUDOURIDINE SYNTHASE; 1.
DR Pfam; PF16198; TruB_C_2; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01080};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01080}.
FT DOMAIN 23..177
FT /note="Pseudouridine synthase II N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01509"
FT DOMAIN 178..221
FT /note="tRNA pseudouridylate synthase B C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16198"
FT ACT_SITE 38
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01080"
SQ SEQUENCE 292 AA; 32256 MW; C6633F704F23A5AA CRC64;
MNGIINLKKE AGMTSHDAVF KLRKILGTKK IGHGGTLDPD VVGVLPIAVG KATRMVEFMQ
DEGKIYEGEI TLGYSTTTED ASGEVIAETP VLSPLDEKLV DEAIASLTGP ITQIPPMYSA
VKVNGRKLYE YARAGQEVER PERQVTIYQF ERTSPISYDG QLARFTFRVK CSKGTYIRTL
SVDLGEKLGY AAHMSHLTRT SAAGLQLEDA LALEEIAEKV EAGQLDFLHP LEIGTGDLVK
VFLTPEEATE VRFGRFIELD QTDKELAAFE DDKLLAILEK RGNLYKPRKV FS
//
