RLUA_ECOLI
ID RLUA_ECOLI Reviewed; 219 AA.
AC P0AA37; P39219; Q2MCG7; Q83MG7;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Dual-specificity RNA pseudouridine synthase RluA {ECO:0000305};
DE EC=5.4.99.28 {ECO:0000269|PubMed:7493321};
DE EC=5.4.99.29 {ECO:0000269|PubMed:7493321};
DE AltName: Full=23S rRNA pseudouridine(746) synthase {ECO:0000305};
DE AltName: Full=Ribosomal large subunit pseudouridine synthase A {ECO:0000305};
DE AltName: Full=rRNA pseudouridylate synthase A {ECO:0000305};
DE AltName: Full=rRNA-uridine isomerase A {ECO:0000305};
DE AltName: Full=tRNA pseudouridine(32) synthase {ECO:0000305};
GN Name=rluA; Synonyms=yabO; OrderedLocusNames=b0058, JW0057;
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;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
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 IDENTIFICATION.
RX PubMed=7958944; DOI=10.1016/0378-1119(94)90688-2;
RA Myler P.J., Venkataraman G.M., Lodes M.J., Stuart K.D.;
RT "A frequently amplified region in Leishmania contains a gene conserved in
RT prokaryotes and eukaryotes.";
RL Gene 148:187-193(1994).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=7493321;
RA Wrzesinski J., Nurse K., Bakin A., Lane B.G., Ofengand J.;
RT "A dual-specificity pseudouridine synthase: an Escherichia coli synthase
RT purified and cloned on the basis of its specificity for psi 746 in 23S RNA
RT is also specific for psi 32 in tRNA(phe).";
RL RNA 1:437-448(1995).
RN [6]
RP MUTAGENESIS OF CYS-117 AND CYS-128.
RC STRAIN=BLR-DE3, and K12 / JM109 / ATCC 53323;
RX PubMed=10529181; DOI=10.1021/bi9913911;
RA Ramamurthy V., Swann S.L., Spedaliere C.J., Mueller E.G.;
RT "Role of cysteine residues in pseudouridine synthases of different
RT families.";
RL Biochemistry 38:13106-13111(1999).
RN [7]
RP FUNCTION, MUTAGENESIS OF ASP-64, AND ACTIVE SITE.
RC STRAIN=BL21-DE3, and K12 / MG1655 / ATCC 47076;
RX PubMed=10383384; DOI=10.1074/jbc.274.27.18880;
RA Raychaudhuri S., Niu L., Conrad J., Lane B.G., Ofengand J.;
RT "Functional effect of deletion and mutation of the Escherichia coli
RT ribosomal RNA and tRNA pseudouridine synthase RluA.";
RL J. Biol. Chem. 274:18880-18886(1999).
RN [8]
RP MUTAGENESIS OF LYS-28 AND PRO-29.
RC STRAIN=BLR-DE3;
RX PubMed=10924141; DOI=10.1021/bi001079n;
RA Spedaliere C.J., Hamilton C.S., Mueller E.G.;
RT "Functional importance of motif I of pseudouridine synthases: mutagenesis
RT of aligned lysine and proline residues.";
RL Biochemistry 39:9459-9465(2000).
CC -!- FUNCTION: Dual specificity enzyme that catalyzes the synthesis of
CC pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32
CC in the anticodon stem and loop of transfer RNAs.
CC {ECO:0000269|PubMed:10383384, ECO:0000269|PubMed:7493321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(32) in tRNA = pseudouridine(32) in tRNA;
CC Xref=Rhea:RHEA:42544, Rhea:RHEA-COMP:10107, Rhea:RHEA-COMP:10108,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.28;
CC Evidence={ECO:0000269|PubMed:7493321};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(746) in 23S rRNA = pseudouridine(746) in 23S rRNA;
CC Xref=Rhea:RHEA:42548, Rhea:RHEA-COMP:10109, Rhea:RHEA-COMP:10110,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.29;
CC Evidence={ECO:0000269|PubMed:7493321};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC73169.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76039.1; -; Genomic_DNA.
DR PIR; B64727; B64727.
DR RefSeq; NP_414600.1; NC_000913.3.
DR RefSeq; WP_000525176.1; NZ_STEB01000010.1.
DR PDB; 2I82; X-ray; 2.05 A; A/B/C/D=3-219.
DR PDBsum; 2I82; -.
DR AlphaFoldDB; P0AA37; -.
DR SMR; P0AA37; -.
DR BioGRID; 4262040; 44.
DR BioGRID; 850621; 3.
DR DIP; DIP-47988N; -.
DR IntAct; P0AA37; 4.
DR STRING; 511145.b0058; -.
DR jPOST; P0AA37; -.
DR PaxDb; P0AA37; -.
DR PRIDE; P0AA37; -.
DR EnsemblBacteria; AAC73169; AAC73169; b0058.
DR EnsemblBacteria; BAE76039; BAE76039; BAE76039.
DR GeneID; 66671653; -.
DR GeneID; 946262; -.
DR KEGG; ecj:JW0057; -.
DR KEGG; eco:b0058; -.
DR PATRIC; fig|1411691.4.peg.2225; -.
DR EchoBASE; EB2493; -.
DR eggNOG; COG0564; Bacteria.
DR HOGENOM; CLU_016902_11_1_6; -.
DR InParanoid; P0AA37; -.
DR OMA; HVSQSRM; -.
DR PhylomeDB; P0AA37; -.
DR BioCyc; EcoCyc:EG12609-MON; -.
DR BioCyc; MetaCyc:EG12609-MON; -.
DR BRENDA; 5.4.99.28; 2026.
DR BRENDA; 5.4.99.29; 2026.
DR EvolutionaryTrace; P0AA37; -.
DR PRO; PR:P0AA37; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:EcoCyc.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0120159; F:rRNA pseudouridine synthase activity; IDA:EcoCyc.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IDA:EcoCyc.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IMP:EcoCyc.
DR GO; GO:0001522; P:pseudouridine synthesis; IMP:EcoliWiki.
DR GO; GO:0009451; P:RNA modification; IMP:EcoliWiki.
DR GO; GO:0006364; P:rRNA processing; IMP:EcoliWiki.
DR GO; GO:0031118; P:rRNA pseudouridine synthesis; IMP:EcoliWiki.
DR GO; GO:0008033; P:tRNA processing; IMP:EcoliWiki.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IMP:EcoCyc.
DR CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00005; rluA_subfam; 1.
DR PROSITE; PS01129; PSI_RLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Reference proteome;
KW rRNA processing; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..219
FT /note="Dual-specificity RNA pseudouridine synthase RluA"
FT /id="PRO_0000162651"
FT ACT_SITE 64
FT /evidence="ECO:0000269|PubMed:10383384"
FT MUTAGEN 28
FT /note="K->M,R: Forms inclusion bodies, indicating
FT precipitation even within the cell."
FT /evidence="ECO:0000269|PubMed:10924141"
FT MUTAGEN 29
FT /note="P->G,L: Reduced structural stability and decrease in
FT activity."
FT /evidence="ECO:0000269|PubMed:10924141"
FT MUTAGEN 64
FT /note="D->N,T: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10383384"
FT MUTAGEN 117
FT /note="C->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:10529181"
FT MUTAGEN 128
FT /note="C->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:10529181"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2I82"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2I82"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:2I82"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 92..102
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2I82"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2I82"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:2I82"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:2I82"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:2I82"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:2I82"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:2I82"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2I82"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:2I82"
SQ SEQUENCE 219 AA; 24861 MW; 2ADCE6D779D8C4AB CRC64;
MGMENYNPPQ EPWLVILYQD DHIMVVNKPS GLLSVPGRLE EHKDSVMTRI QRDYPQAESV
HRLDMATSGV IVVALTKAAE RELKRQFRER EPKKQYVARV WGHPSPAEGL VDLPLICDWP
NRPKQKVCYE TGKPAQTEYE VVEYAADNTA RVVLKPITGR SHQLRVHMLA LGHPILGDRF
YASPEARAMA PRLLLHAEML TITHPAYGNS MTFKAPADF
