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Protein

Ribosomal small subunit pseudouridine synthase A

Gene

rsuA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA.2 Publications

Catalytic activityi

16S rRNA uridine(516) = 16S rRNA pseudouridine(516).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei102 – 1021Nucleophile1 Publication

GO - Molecular functioni

  • pseudouridine synthase activity Source: EcoCyc
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • enzyme-directed rRNA pseudouridine synthesis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12044-MONOMER.
ECOL316407:JW2171-MONOMER.
MetaCyc:EG12044-MONOMER.
BRENDAi5.4.99.19. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal small subunit pseudouridine synthase A (EC:5.4.99.19)
Alternative name(s):
16S pseudouridylate 516 synthase
16S rRNA pseudouridine(516) synthase
rRNA pseudouridylate synthase A
rRNA-uridine isomerase A
Gene namesi
Name:rsuA
Synonyms:yejD
Ordered Locus Names:b2183, JW2171
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12044. rsuA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi102 – 1021D → N or T: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231Ribosomal small subunit pseudouridine synthase APRO_0000099966Add
BLAST

Proteomic databases

PaxDbiP0AA43.
PRIDEiP0AA43.

2D gel databases

SWISS-2DPAGEP0AA43.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
rpsJP0A7R52EBI-557810,EBI-544602

Protein-protein interaction databases

BioGridi4260474. 7 interactions.
DIPiDIP-35902N.
IntActiP0AA43. 40 interactions.
MINTiMINT-1221744.
STRINGi511145.b2183.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Helixi15 – 239Combined sources
Turni24 – 263Combined sources
Beta strandi27 – 293Combined sources
Beta strandi47 – 493Combined sources
Beta strandi52 – 543Combined sources
Beta strandi62 – 676Combined sources
Beta strandi72 – 765Combined sources
Beta strandi78 – 803Combined sources
Helixi83 – 864Combined sources
Helixi92 – 943Combined sources
Beta strandi96 – 994Combined sources
Beta strandi106 – 1138Combined sources
Helixi115 – 1228Combined sources
Beta strandi130 – 1389Combined sources
Helixi144 – 1507Combined sources
Beta strandi165 – 1706Combined sources
Beta strandi173 – 1797Combined sources
Helixi185 – 1928Combined sources
Beta strandi197 – 2059Combined sources
Beta strandi219 – 2213Combined sources
Helixi224 – 2274Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KSKX-ray2.00A1-231[»]
1KSLX-ray2.10A1-231[»]
1KSVX-ray2.65A1-231[»]
ProteinModelPortaliP0AA43.
SMRiP0AA43. Positions 1-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AA43.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6868S4 RNA-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the pseudouridine synthase RsuA family.Curated
Contains 1 S4 RNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105I08. Bacteria.
COG1187. LUCA.
HOGENOMiHOG000044954.
InParanoidiP0AA43.
KOiK06183.
OMAiCTVTLHE.
OrthoDBiEOG6130DV.
PhylomeDBiP0AA43.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
InterProiIPR020103. PsdUridine_synth_cat_dom.
IPR000748. PsdUridine_synth_RsuA/RluB/E/F.
IPR018496. PsdUridine_synth_RsuA/RluB_CS.
IPR006145. PsdUridine_synth_RsuA/RluD.
IPR002942. S4_RNA-bd.
[Graphical view]
PfamiPF00849. PseudoU_synth_2. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM00363. S4. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
TIGRFAMsiTIGR00093. TIGR00093. 1 hit.
PROSITEiPS01149. PSI_RSU. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AA43-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLDKFIAQQ LGVSRAIAGR EIRGNRVTVD GEIVRNAAFK LLPEHDVAYD
60 70 80 90 100
GNPLAQQHGP RYFMLNKPQG YVCSTDDPDH PTVLYFLDEP VAWKLHAAGR
110 120 130 140 150
LDIDTTGLVL MTDDGQWSHR ITSPRHHCEK TYLVTLESPV ADDTAEQFAK
160 170 180 190 200
GVQLHNEKDL TKPAVLEVIT PTQVRLTISE GRYHQVKRMF AAVGNHVVEL
210 220 230
HRERIGGITL DADLAPGEYR PLTEEEIASV V
Length:231
Mass (Da):25,865
Last modified:September 13, 2005 - v1
Checksum:i04EB7154931C58F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00008 Genomic DNA. Translation: AAA16377.1.
U00096 Genomic DNA. Translation: AAC75244.1.
AP009048 Genomic DNA. Translation: BAE76648.1.
PIRiF64987.
RefSeqiNP_416688.1. NC_000913.3.
WP_001234850.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75244; AAC75244; b2183.
BAE76648; BAE76648; BAE76648.
GeneIDi945378.
KEGGiecj:JW2171.
eco:b2183.
PATRICi32119721. VBIEscCol129921_2271.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00008 Genomic DNA. Translation: AAA16377.1.
U00096 Genomic DNA. Translation: AAC75244.1.
AP009048 Genomic DNA. Translation: BAE76648.1.
PIRiF64987.
RefSeqiNP_416688.1. NC_000913.3.
WP_001234850.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KSKX-ray2.00A1-231[»]
1KSLX-ray2.10A1-231[»]
1KSVX-ray2.65A1-231[»]
ProteinModelPortaliP0AA43.
SMRiP0AA43. Positions 1-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260474. 7 interactions.
DIPiDIP-35902N.
IntActiP0AA43. 40 interactions.
MINTiMINT-1221744.
STRINGi511145.b2183.

2D gel databases

SWISS-2DPAGEP0AA43.

Proteomic databases

PaxDbiP0AA43.
PRIDEiP0AA43.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75244; AAC75244; b2183.
BAE76648; BAE76648; BAE76648.
GeneIDi945378.
KEGGiecj:JW2171.
eco:b2183.
PATRICi32119721. VBIEscCol129921_2271.

Organism-specific databases

EchoBASEiEB1978.
EcoGeneiEG12044. rsuA.

Phylogenomic databases

eggNOGiENOG4105I08. Bacteria.
COG1187. LUCA.
HOGENOMiHOG000044954.
InParanoidiP0AA43.
KOiK06183.
OMAiCTVTLHE.
OrthoDBiEOG6130DV.
PhylomeDBiP0AA43.

Enzyme and pathway databases

BioCyciEcoCyc:EG12044-MONOMER.
ECOL316407:JW2171-MONOMER.
MetaCyc:EG12044-MONOMER.
BRENDAi5.4.99.19. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AA43.
PROiP0AA43.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
InterProiIPR020103. PsdUridine_synth_cat_dom.
IPR000748. PsdUridine_synth_RsuA/RluB/E/F.
IPR018496. PsdUridine_synth_RsuA/RluB_CS.
IPR006145. PsdUridine_synth_RsuA/RluD.
IPR002942. S4_RNA-bd.
[Graphical view]
PfamiPF00849. PseudoU_synth_2. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM00363. S4. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
TIGRFAMsiTIGR00093. TIGR00093. 1 hit.
PROSITEiPS01149. PSI_RSU. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification, cloning, and properties of the 16S RNA pseudouridine 516 synthase from Escherichia coli."
    Wrzesinski J., Bakin A., Nurse K., Lane B.G., Ofengand J.
    Biochemistry 34:8904-8913(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  2. Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
    Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / BHB2600.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "16S ribosomal RNA pseudouridine synthase RsuA of Escherichia coli: deletion, mutation of the conserved Asp102 residue, and sequence comparison among all other pseudouridine synthases."
    Conrad J., Niu L., Rudd K., Lane B.G., Ofengand J.
    RNA 5:751-763(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-102.
    Strain: BL21-DE3 and K12 / MG1655 / ATCC 47076.
  6. "Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP."
    Sivaraman J., Sauve V., Larocque R., Stura E.A., Schrag J.D., Cygler M., Matte A.
    Nat. Struct. Biol. 9:353-358(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH URACIL AND UMP, ACTIVE SITE.

Entry informationi

Entry nameiRSUA_ECOLI
AccessioniPrimary (citable) accession number: P0AA43
Secondary accession number(s): P33918, Q2MAQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: January 20, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.