ID RLUC_ECOLI Reviewed; 319 AA.
AC P0AA39; P23851;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Ribosomal large subunit pseudouridine synthase C;
DE EC=5.4.99.24 {ECO:0000269|PubMed:9660827};
DE AltName: Full=23S rRNA pseudouridine(955/2504/2580) synthase;
DE AltName: Full=rRNA pseudouridylate synthase C;
DE AltName: Full=rRNA-uridine isomerase C;
GN Name=rluC {ECO:0000303|PubMed:9660827}; Synonyms=yceC;
GN OrderedLocusNames=b1086, JW1072;
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=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(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 1-285.
RC STRAIN=K12;
RX PubMed=1704367; DOI=10.1016/s0021-9258(18)49924-3;
RA Claverie-Martin F., Diaz-Torres M., Yancey S.D., Kushner S.R.;
RT "Analysis of the altered mRNA stability (ams) gene from Escherichia coli.
RT Nucleotide sequence, transcriptional analysis, and homology of its product
RT to MRP3, a mitochondrial ribosomal protein from Neurospora crassa.";
RL J. Biol. Chem. 266:2843-2851(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 260-319.
RC STRAIN=K12;
RX PubMed=1447160; DOI=10.1128/jb.174.23.7873-7874.1992;
RA Oh W., Larson T.J.;
RT "Physical locations of genes in the rne (ams)-rpmF-plsX-fab region of the
RT Escherichia coli K-12 chromosome.";
RL J. Bacteriol. 174:7873-7874(1992).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9660827; DOI=10.1074/jbc.273.29.18562;
RA Conrad J., Sun D., Englund N., Ofengand J.;
RT "The rluC gene of Escherichia coli codes for a pseudouridine synthase that
RT is solely responsible for synthesis of pseudouridine at positions 955,
RT 2504, and 2580 in 23 S ribosomal RNA.";
RL J. Biol. Chem. 273:18562-18566(1998).
RN [7]
RP PROBABLE ACTIVE SITE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-144.
RC STRAIN=K12;
RX PubMed=18820021; DOI=10.1128/jb.00835-08;
RA Krishnan K., Flower A.M.;
RT "Suppression of DeltabipA phenotypes in Escherichia coli by abolishment of
RT pseudouridylation at specific sites on the 23S rRNA.";
RL J. Bacteriol. 190:7675-7683(2008).
RN [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=25777676; DOI=10.1128/jb.00023-15;
RA Choudhury P., Flower A.M.;
RT "Efficient assembly of ribosomes is inhibited by deletion of bipA in
RT Escherichia coli.";
RL J. Bacteriol. 197:1819-1827(2015).
RN [9]
RP CRYSTALLIZATION OF 89-319, AND PROTEIN SEQUENCE OF 89-98.
RC STRAIN=BL21-DE3;
RX PubMed=10089432; DOI=10.1107/s090744499801021x;
RA Corollo D., Blair-Johnson M., Conrad J., Fiedler T., Sun D., Wang L.,
RA Ofengand J., Fenna R.;
RT "Crystallization and characterization of a fragment of pseudouridine
RT synthase RluC from Escherichia coli.";
RL Acta Crystallogr. D 55:302-304(1999).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil at
CC positions 955, 2504 and 2580 in 23S ribosomal RNA.
CC {ECO:0000269|PubMed:9660827}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(955/2504/2580) in 23S rRNA =
CC pseudouridine(955/2504/2580) in 23S rRNA; Xref=Rhea:RHEA:42528,
CC Rhea:RHEA-COMP:10099, Rhea:RHEA-COMP:10100, ChEBI:CHEBI:65314,
CC ChEBI:CHEBI:65315; EC=5.4.99.24;
CC Evidence={ECO:0000269|PubMed:9660827};
CC -!- DISRUPTION PHENOTYPE: No visible growth phenotype (PubMed:9660827). An
CC rluC deletion suppresses a bipA deletion; in a double rluC-bipA
CC deletion the cold-sensitive growth and ribosome assembly defects at 20
CC degrees Celsius due to bipA are fully suppressed and decreased capsule
CC synthesis is partially suppressed (PubMed:18820021, PubMed:25777676).
CC {ECO:0000269|PubMed:18820021, ECO:0000269|PubMed:25777676,
CC ECO:0000269|PubMed:9660827}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74170.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35894.1; -; Genomic_DNA.
DR EMBL; M62747; AAA23442.1; -; Genomic_DNA.
DR EMBL; M96791; AAA23828.1; -; Genomic_DNA.
DR PIR; C64852; C64852.
DR RefSeq; NP_415604.1; NC_000913.3.
DR RefSeq; WP_000846343.1; NZ_STEB01000016.1.
DR PDB; 1V9K; X-ray; 2.00 A; A/B=92-319.
DR PDB; 1XPI; X-ray; 2.20 A; A/B=89-319.
DR PDBsum; 1V9K; -.
DR PDBsum; 1XPI; -.
DR AlphaFoldDB; P0AA39; -.
DR SMR; P0AA39; -.
DR BioGRID; 4261025; 63.
DR BioGRID; 850009; 1.
DR DIP; DIP-47832N; -.
DR IntAct; P0AA39; 70.
DR STRING; 511145.b1086; -.
DR jPOST; P0AA39; -.
DR PaxDb; 511145-b1086; -.
DR EnsemblBacteria; AAC74170; AAC74170; b1086.
DR GeneID; 75203672; -.
DR GeneID; 945637; -.
DR KEGG; ecj:JW1072; -.
DR KEGG; eco:b1086; -.
DR PATRIC; fig|1411691.4.peg.1182; -.
DR EchoBASE; EB1108; -.
DR eggNOG; COG0564; Bacteria.
DR HOGENOM; CLU_016902_1_1_6; -.
DR InParanoid; P0AA39; -.
DR OMA; NKGRVKP; -.
DR OrthoDB; 9807829at2; -.
DR PhylomeDB; P0AA39; -.
DR BioCyc; EcoCyc:EG11118-MONOMER; -.
DR BioCyc; MetaCyc:EG11118-MONOMER; -.
DR BRENDA; 5.4.99.24; 2026.
DR EvolutionaryTrace; P0AA39; -.
DR PRO; PR:P0AA39; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0120159; F:rRNA pseudouridine synthase activity; IDA:EcoCyc.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IDA:EcoliWiki.
DR CDD; cd02869; PseudoU_synth_RluA_like; 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; IPR006224; PsdUridine_synth_RluA-like_CS.
DR InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR NCBIfam; TIGR00005; rluA_subfam; 1.
DR PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR PANTHER; PTHR21600:SF93; PSEUDOURIDYLATE SYNTHASE RPUSD4, MITOCHONDRIAL; 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; PS01129; PSI_RLU; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Reference proteome;
KW RNA-binding; rRNA processing.
FT CHAIN 1..319
FT /note="Ribosomal large subunit pseudouridine synthase C"
FT /id="PRO_0000162667"
FT DOMAIN 20..83
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT ACT_SITE 144
FT /evidence="ECO:0000305|PubMed:18820021"
FT MUTAGEN 144
FT /note="D->T: Does not restore cold-sensitive growth to a
FT double bipA-rluC deletion."
FT /evidence="ECO:0000269|PubMed:18820021"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:1XPI"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1V9K"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:1V9K"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1V9K"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:1V9K"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1V9K"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:1V9K"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:1V9K"
FT STRAND 172..182
FT /evidence="ECO:0007829|PDB:1V9K"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1V9K"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1V9K"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:1V9K"
FT STRAND 227..238
FT /evidence="ECO:0007829|PDB:1V9K"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:1V9K"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1V9K"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:1V9K"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:1V9K"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:1V9K"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:1V9K"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:1V9K"
SQ SEQUENCE 319 AA; 36027 MW; 19C8D05E426F0344 CRC64;
MKTETPSVKI VAITADEAGQ RIDNFLRTQL KGVPKSMIYR ILRKGEVRVN KKRIKPEYKL
EAGDEVRIPP VRVAEREEEA VSPHLQKVAA LADVILYEDD HILVLNKPSG TAVHGGSGLS
FGVIEGLRAL RPEARFLELV HRLDRDTSGV LLVAKKRSAL RSLHEQLREK GMQKDYLALV
RGQWQSHVKS VQAPLLKNIL QSGERIVRVS QEGKPSETRF KVEERYAFAT LVRCSPVTGR
THQIRVHTQY AGHPIAFDDR YGDREFDRQL TEAGTGLNRL FLHAAALKFT HPGTGEVMRI
EAPMDEGLKR CLQKLRNAR
//
