ID   RLUB_ECOLI              Reviewed;         291 AA.
AC   P37765;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   27-MAR-2024, entry version 172.
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; Synonyms=yciL; OrderedLocusNames=b1269, JW1261;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-243.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Milkman R., McKane M.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-291.
RC   STRAIN=K12;
RX   PubMed=2644187; DOI=10.1128/jb.171.1.154-161.1989;
RA   Lundrigan M.D., Kadner R.J.;
RT   "Altered cobalamin metabolism in Escherichia coli btuR mutants affects btuB
RT   gene regulation.";
RL   J. Bacteriol. 171:154-161(1989).
RN   [6]
RP   IDENTIFICATION.
RX   PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA   Borodovsky M., Rudd K.E., Koonin E.V.;
RT   "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT   genome.";
RL   Nucleic Acids Res. 22:4756-4767(1994).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-110.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=11720289;
RA   Del Campo M., Kaya Y., Ofengand J.;
RT   "Identification and site of action of the remaining four putative
RT   pseudouridine synthases in Escherichia coli.";
RL   RNA 7:1603-1615(2001).
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-2605
CC       in 23S ribosomal RNA. {ECO:0000269|PubMed:11720289}.
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         Evidence={ECO:0000269|PubMed:11720289};
CC   -!- INTERACTION:
CC       P37765; P75864: rlmL; NbExp=3; IntAct=EBI-561550, EBI-547718;
CC       P37765; P02359: rpsG; NbExp=4; IntAct=EBI-561550, EBI-543074;
CC       P37765; P21507: srmB; NbExp=6; IntAct=EBI-561550, EBI-546628;
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=M21528; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U00096; AAC74351.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14806.1; -; Genomic_DNA.
DR   EMBL; U18111; AAB59990.1; -; Genomic_DNA.
DR   EMBL; M21528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; H64874; H64874.
DR   RefSeq; NP_415785.1; NC_000913.3.
DR   RefSeq; WP_001291217.1; NZ_SSZK01000031.1.
DR   PDB; 4LAB; X-ray; 2.50 A; A=1-251.
DR   PDB; 4LGT; X-ray; 1.30 A; A/D=1-251.
DR   PDBsum; 4LAB; -.
DR   PDBsum; 4LGT; -.
DR   AlphaFoldDB; P37765; -.
DR   SMR; P37765; -.
DR   BioGRID; 4259574; 50.
DR   BioGRID; 850207; 3.
DR   DIP; DIP-11585N; -.
DR   IntAct; P37765; 79.
DR   STRING; 511145.b1269; -.
DR   jPOST; P37765; -.
DR   PaxDb; 511145-b1269; -.
DR   EnsemblBacteria; AAC74351; AAC74351; b1269.
DR   GeneID; 83576465; -.
DR   GeneID; 945840; -.
DR   KEGG; ecj:JW1261; -.
DR   KEGG; eco:b1269; -.
DR   PATRIC; fig|1411691.4.peg.1015; -.
DR   EchoBASE; EB2329; -.
DR   eggNOG; COG1187; Bacteria.
DR   HOGENOM; CLU_024979_1_1_6; -.
DR   InParanoid; P37765; -.
DR   OMA; QKEICRV; -.
DR   OrthoDB; 9807213at2; -.
DR   PhylomeDB; P37765; -.
DR   BioCyc; EcoCyc:EG12433-MONOMER; -.
DR   BioCyc; MetaCyc:EG12433-MONOMER; -.
DR   BRENDA; 5.4.99.22; 2026.
DR   PRO; PR:P37765; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0120159; F:rRNA pseudouridine synthase activity; IMP:EcoCyc.
DR   GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IMP:EcoCyc.
DR   CDD; cd02556; PseudoU_synth_RluB; 1.
DR   CDD; cd00165; S4; 1.
DR   Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
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   NCBIfam; TIGR00093; pseudouridine synthase; 1.
DR   PANTHER; PTHR47683; PSEUDOURIDINE SYNTHASE FAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47683:SF3; RIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B; 1.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR   PROSITE; PS01149; PSI_RSU; 1.
DR   PROSITE; PS50889; S4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Isomerase; Reference proteome; RNA-binding; rRNA processing.
FT   CHAIN           1..291
FT                   /note="Ribosomal large subunit pseudouridine synthase B"
FT                   /id="PRO_0000099983"
FT   DOMAIN          3..75
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT   REGION          256..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        110
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         110
FT                   /note="D->N,T: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11720289"
FT   HELIX           5..11
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   HELIX           17..25
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          69..74
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   TURN            91..94
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          104..107
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          114..121
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   HELIX           123..130
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          138..146
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   HELIX           150..158
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          170..178
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          181..190
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   HELIX           195..202
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          206..215
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:4LGT"
FT   HELIX           234..243
FT                   /evidence="ECO:0007829|PDB:4LGT"
SQ   SEQUENCE   291 AA;  32711 MW;  101DF8FD55CB557D CRC64;
     MSEKLQKVLA RAGHGSRREI ESIIEAGRVS VDGKIAKLGD RVEVTPGLKI RIDGHLISVR
     ESAEQICRVL AYYKPEGELC TRNDPEGRPT VFDRLPKLRG ARWIAVGRLD VNTCGLLLFT
     TDGELANRLM HPSREVEREY AVRVFGQVDD AKLRDLSRGV QLEDGPAAFK TIKFSGGEGI
     NQWYNVTLTE GRNREVRRLW EAVGVQVSRL IRVRYGDIPL PKGLPRGGWT ELDLAQTNYL
     RELVELPPET SSKVAVEKDR RRMKANQIRR AVKRHSQVSG GRRSGGRNNN G
//