RSUA_ECOLI
ID RSUA_ECOLI Reviewed; 231 AA.
AC P0AA43; P33918; Q2MAQ8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Ribosomal small subunit pseudouridine synthase A;
DE EC=5.4.99.19;
DE AltName: Full=16S pseudouridylate 516 synthase;
DE AltName: Full=16S rRNA pseudouridine(516) synthase;
DE AltName: Full=rRNA pseudouridylate synthase A;
DE AltName: Full=rRNA-uridine isomerase A;
GN Name=rsuA; Synonyms=yejD; OrderedLocusNames=b2183, JW2171;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=7612632; DOI=10.1021/bi00027a043;
RA Wrzesinski J., Bakin A., Nurse K., Lane B.G., Ofengand J.;
RT "Purification, cloning, and properties of the 16S RNA pseudouridine 516
RT synthase from Escherichia coli.";
RL Biochemistry 34:8904-8913(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-102.
RC STRAIN=BL21-DE3, and K12 / MG1655 / ATCC 47076;
RX PubMed=10376875; DOI=10.1017/s1355838299990167;
RA Conrad J., Niu L., Rudd K., Lane B.G., Ofengand J.;
RT "16S ribosomal RNA pseudouridine synthase RsuA of Escherichia coli:
RT deletion, mutation of the conserved Asp102 residue, and sequence comparison
RT among all other pseudouridine synthases.";
RL RNA 5:751-763(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH URACIL AND UMP, AND
RP ACTIVE SITE.
RX PubMed=11953756; DOI=10.1038/nsb788;
RA Sivaraman J., Sauve V., Larocque R., Stura E.A., Schrag J.D., Cygler M.,
RA Matte A.;
RT "Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and
RT UMP.";
RL Nat. Struct. Biol. 9:353-358(2002).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-516 in
CC 16S ribosomal RNA. {ECO:0000269|PubMed:10376875,
CC ECO:0000269|PubMed:7612632}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(516) in 16S rRNA = pseudouridine(516) in 16S rRNA;
CC Xref=Rhea:RHEA:38867, Rhea:RHEA-COMP:10089, Rhea:RHEA-COMP:10090,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.19;
CC Evidence={ECO:0000269|PubMed:10376875, ECO:0000269|PubMed:7612632};
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P0AA43; P0A7R5: rpsJ; NbExp=3; IntAct=EBI-557810, EBI-544602;
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC {ECO:0000305}.
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DR EMBL; U00008; AAA16377.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75244.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76648.1; -; Genomic_DNA.
DR PIR; F64987; F64987.
DR RefSeq; NP_416688.1; NC_000913.3.
DR RefSeq; WP_001234850.1; NZ_STEB01000002.1.
DR PDB; 1KSK; X-ray; 2.00 A; A=1-231.
DR PDB; 1KSL; X-ray; 2.10 A; A=1-231.
DR PDB; 1KSV; X-ray; 2.65 A; A=1-231.
DR PDBsum; 1KSK; -.
DR PDBsum; 1KSL; -.
DR PDBsum; 1KSV; -.
DR AlphaFoldDB; P0AA43; -.
DR SMR; P0AA43; -.
DR BioGRID; 4260474; 48.
DR DIP; DIP-35902N; -.
DR IntAct; P0AA43; 40.
DR STRING; 511145.b2183; -.
DR DrugBank; DB03419; Uracil.
DR DrugBank; DB03685; Uridine monophosphate.
DR SWISS-2DPAGE; P0AA43; -.
DR jPOST; P0AA43; -.
DR PaxDb; P0AA43; -.
DR PRIDE; P0AA43; -.
DR EnsemblBacteria; AAC75244; AAC75244; b2183.
DR EnsemblBacteria; BAE76648; BAE76648; BAE76648.
DR GeneID; 66673920; -.
DR GeneID; 945378; -.
DR KEGG; ecj:JW2171; -.
DR KEGG; eco:b2183; -.
DR PATRIC; fig|1411691.4.peg.53; -.
DR EchoBASE; EB1978; -.
DR eggNOG; COG1187; Bacteria.
DR HOGENOM; CLU_024979_1_2_6; -.
DR InParanoid; P0AA43; -.
DR OMA; HVPKTYE; -.
DR PhylomeDB; P0AA43; -.
DR BioCyc; EcoCyc:EG12044-MON; -.
DR BioCyc; MetaCyc:EG12044-MON; -.
DR BRENDA; 5.4.99.19; 2026.
DR EvolutionaryTrace; P0AA43; -.
DR PRO; PR:P0AA43; -.
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; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Reference proteome;
KW RNA-binding; rRNA processing.
FT CHAIN 1..231
FT /note="Ribosomal small subunit pseudouridine synthase A"
FT /id="PRO_0000099966"
FT DOMAIN 1..68
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:11953756"
FT MUTAGEN 102
FT /note="D->N,T: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10376875"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:1KSK"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:1KSK"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1KSV"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1KSK"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1KSK"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:1KSK"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1KSK"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:1KSK"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 197..205
FT /evidence="ECO:0007829|PDB:1KSK"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1KSK"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:1KSK"
SQ SEQUENCE 231 AA; 25865 MW; 04EB7154931C58F7 CRC64;
MRLDKFIAQQ LGVSRAIAGR EIRGNRVTVD GEIVRNAAFK LLPEHDVAYD GNPLAQQHGP
RYFMLNKPQG YVCSTDDPDH PTVLYFLDEP VAWKLHAAGR LDIDTTGLVL MTDDGQWSHR
ITSPRHHCEK TYLVTLESPV ADDTAEQFAK GVQLHNEKDL TKPAVLEVIT PTQVRLTISE
GRYHQVKRMF AAVGNHVVEL HRERIGGITL DADLAPGEYR PLTEEEIASV V
