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TRUB_LISMO
ID   TRUB_LISMO              Reviewed;         304 AA.
AC   Q8Y7F3;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=lmo1328;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591978; CAC99406.1; -; Genomic_DNA.
DR   PIR; AH1240; AH1240.
DR   RefSeq; NP_464853.1; NC_003210.1.
DR   RefSeq; WP_010990096.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y7F3; -.
DR   SMR; Q8Y7F3; -.
DR   STRING; 169963.lmo1328; -.
DR   PaxDb; Q8Y7F3; -.
DR   EnsemblBacteria; CAC99406; CAC99406; CAC99406.
DR   GeneID; 987709; -.
DR   KEGG; lmo:lmo1328; -.
DR   PATRIC; fig|169963.11.peg.1365; -.
DR   eggNOG; COG0130; Bacteria.
DR   HOGENOM; CLU_032087_0_1_9; -.
DR   OMA; ELQFIRW; -.
DR   PhylomeDB; Q8Y7F3; -.
DR   BioCyc; LMON169963:LMO1328-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR   GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
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..304
FT                   /note="tRNA pseudouridine synthase B"
FT                   /id="PRO_0000121859"
FT   ACT_SITE        38
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   304 AA;  33769 MW;  F484C48B46B3DCC5 CRC64;
     MNGIIPLWKE RGMTSHDCVY KLRKILHTKK VGHTGTLDPE VEGVLPICIG RATKLAEYVT
     DEGKVYVAEI TLGKSTTTED ATGETVNTKE LAEISAAELQ AALTKLTGKI TQIPPMFSAV
     KVNGKKLYEY ARAGIEVERP SRQVDIYSLI RLDGDTALNQ SNPTFQLEIA CGKGTYIRTL
     AVMIGELLGY PAHMSKLERT RSGFFKKEDC LTLTEIDEMM QASDSSFLYP LEKGIESMAK
     LVIEEEVYAK VLNGGLLPTS LFAEVENEPR AALIFKDKLT AIYKPHPEKK DLWKPEKVIE
     LNQA
 
 
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