ID   RLUB_XANCP              Reviewed;         492 AA.
AC   Q8P8M6;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Ribosomal large subunit pseudouridine synthase B;
DE            EC=5.4.99.22;
DE   AltName: Full=23S rRNA pseudouridine(2605) synthase;
DE   AltName: Full=rRNA pseudouridylate synthase B;
DE   AltName: Full=rRNA-uridine isomerase B;
GN   Name=rluB; OrderedLocusNames=XCC2214;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-2605
CC       in 23S ribosomal RNA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(2605) in 23S rRNA = pseudouridine(2605) in 23S rRNA;
CC         Xref=Rhea:RHEA:42520, Rhea:RHEA-COMP:10095, Rhea:RHEA-COMP:10096,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.22;
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC       {ECO:0000305}.
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DR   EMBL; AE008922; AAM41494.1; -; Genomic_DNA.
DR   RefSeq; NP_637570.1; NC_003902.1.
DR   AlphaFoldDB; Q8P8M6; -.
DR   SMR; Q8P8M6; -.
DR   STRING; 340.xcc-b100_1966; -.
DR   EnsemblBacteria; AAM41494; AAM41494; XCC2214.
DR   KEGG; xcc:XCC2214; -.
DR   PATRIC; fig|190485.4.peg.2363; -.
DR   eggNOG; COG1187; Bacteria.
DR   HOGENOM; CLU_024979_5_2_6; -.
DR   OMA; HDWFRIV; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0120159; F:rRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IEA:UniProt.
DR   CDD; cd00165; S4; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   Gene3D; 3.30.70.1560; -; 1.
DR   Gene3D; 3.30.70.580; -; 1.
DR   InterPro; IPR042092; PsdUridine_s_RsuA/RluB/E/F_cat.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR   InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F.
DR   InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00093; TIGR00093; 1.
DR   PROSITE; PS01149; PSI_RSU; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome; RNA-binding; rRNA processing.
FT   CHAIN           1..492
FT                   /note="Ribosomal large subunit pseudouridine synthase B"
FT                   /id="PRO_0000099996"
FT   DOMAIN          28..97
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..338
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        132
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   492 AA;  53021 MW;  07883D922E50F6CB CRC64;
     MSDTPRKLSL NKLSLKRDSA PEAPKLEERL HKVLAQAGLG SRRALEQRIA DGLIKVNGAV
     AQTGMSVRSG DKIELDGRSF VASALTESSR VLVYNKPEGE VTTREDPEGR PTVFESLPAL
     KGSRWIAIGR LDINTTGLLL LTTDGELANA MMHPSYEVER EYVVRVRAPE GEEKVPDSMI
     ERLSRGVLLE DGGAKFDEIE RIGGTDSHDW FRVVVKEGRN REVRRLWESQ GCQVSRLKRT
     RYGKVSLPRE LLRGQSVELA QEKVDALRAE LKLEEGAPSA LTLQPVIGQR RAAKSTVHVS
     RDGRSNAYVN GQTSGADEGR ELRRFDNLRE DRGGRGGRGK PGGFKGGLTV SGEAAAKQSQ
     QRPFKQRGPA KGDRSLPDGN PAAFRSWYVP DGVSTGPSGH RNAGPGGAGT GQPRPYAKKG
     PGGARPGAGG QGRGAAGGQG QSQGQGQGQR KHPYGHPGNA PSFPSDHANP GFSPYGAARP
     ANESYKRRPP RH