RLUB_ECOLI
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 03-AUG-2022, entry version 163.
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; Proteobacteria; 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; P37765; -.
DR PRIDE; P37765; -.
DR EnsemblBacteria; AAC74351; AAC74351; b1269.
DR EnsemblBacteria; BAA14806; BAA14806; BAA14806.
DR GeneID; 60668690; -.
DR GeneID; 67417413; -.
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; SMEFAPF; -.
DR PhylomeDB; P37765; -.
DR BioCyc; EcoCyc:EG12433-MON; -.
DR BioCyc; MetaCyc:EG12433-MON; -.
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; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 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 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 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
