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Protein

Heat shock protein 15

Gene

hslR

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

Functioni

Involved in the recycling of free 50S ribosomal subunits that still carry a nascent chain. Binds RNA more specifically than DNA. Binds with very high affinity to the free 50S ribosomal subunit. Does not bind it when it is part of the 70S ribosome.

GO - Molecular functioni

  • DNA binding Source: EcoCyc
  • pseudouridine synthase activity Source: GO_Central
  • ribosomal large subunit binding Source: EcoCyc
  • single-stranded RNA binding Source: EcoCyc

GO - Biological processi

  • cellular response to heat Source: EcoCyc
  • enzyme-directed rRNA pseudouridine synthesis Source: GO_Central
  • response to heat Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7743-MONOMER.
ECOL316407:JW3363-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein 15
Short name:
HSP15
Gene namesi
Name:hslR
Synonyms:yrfH
Ordered Locus Names:b3400, JW3363
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12929. hslR.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 133133Heat shock protein 15PRO_0000201741Add
BLAST

Proteomic databases

PaxDbiP0ACG8.

Expressioni

Inductioni

By heat shock.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
malTP069932EBI-562824,EBI-542934
rpsBP0A7V02EBI-562824,EBI-543439
ykgNQ79E922EBI-562824,EBI-9131095

Protein-protein interaction databases

BioGridi4260979. 237 interactions.
DIPiDIP-48014N.
IntActiP0ACG8. 37 interactions.
STRINGi511145.b3400.

Structurei

Secondary structure

1
133
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 177Combined sources
Beta strandi20 – 234Combined sources
Helixi24 – 329Combined sources
Beta strandi36 – 383Combined sources
Beta strandi54 – 596Combined sources
Beta strandi62 – 687Combined sources
Beta strandi70 – 734Combined sources
Helixi78 – 814Combined sources
Helixi82 – 843Combined sources
Beta strandi85 – 873Combined sources
Helixi89 – 10618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DM9X-ray2.00A/B1-133[»]
3BBUelectron microscopy10.00A5-108[»]
ProteinModelPortaliP0ACG8.
SMRiP0ACG8. Positions 4-110.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACG8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 7163S4 RNA-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the HSP15 family.Curated
Contains 1 S4 RNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105VEJ. Bacteria.
COG1188. LUCA.
HOGENOMiHOG000216822.
InParanoidiP0ACG8.
KOiK04762.
OMAiRFYKTRT.
OrthoDBiEOG64NB4B.
PhylomeDBiP0ACG8.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
InterProiIPR025708. HSP15.
IPR002942. S4_RNA-bd.
[Graphical view]
PfamiPF01479. S4. 1 hit.
[Graphical view]
PIRSFiPIRSF016821. HSP15. 1 hit.
SMARTiSM00363. S4. 1 hit.
[Graphical view]
PROSITEiPS50889. S4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ACG8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEKPAVEVR LDKWLWAARF YKTRALAREM IEGGKVHYNG QRSKPSKIVE
60 70 80 90 100
LNATLTLRQG NDERTVIVKA ITEQRRPASE AALLYEETAE SVEKREKMAL
110 120 130
ARKLNALTMP HPDRRPDKKE RRDLLRFKHG DSE
Length:133
Mass (Da):15,496
Last modified:November 22, 2005 - v1
Checksum:i4B3D40FAECC42D5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA58197.1.
U00096 Genomic DNA. Translation: AAC76425.1.
AP009048 Genomic DNA. Translation: BAE77891.1.
PIRiC65135.
RefSeqiNP_417859.1. NC_000913.3.
WP_000660483.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76425; AAC76425; b3400.
BAE77891; BAE77891; BAE77891.
GeneIDi947912.
KEGGiecj:JW3363.
eco:b3400.
PATRICi32122234. VBIEscCol129921_3494.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA58197.1.
U00096 Genomic DNA. Translation: AAC76425.1.
AP009048 Genomic DNA. Translation: BAE77891.1.
PIRiC65135.
RefSeqiNP_417859.1. NC_000913.3.
WP_000660483.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DM9X-ray2.00A/B1-133[»]
3BBUelectron microscopy10.00A5-108[»]
ProteinModelPortaliP0ACG8.
SMRiP0ACG8. Positions 4-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260979. 237 interactions.
DIPiDIP-48014N.
IntActiP0ACG8. 37 interactions.
STRINGi511145.b3400.

Proteomic databases

PaxDbiP0ACG8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76425; AAC76425; b3400.
BAE77891; BAE77891; BAE77891.
GeneIDi947912.
KEGGiecj:JW3363.
eco:b3400.
PATRICi32122234. VBIEscCol129921_3494.

Organism-specific databases

EchoBASEiEB2765.
EcoGeneiEG12929. hslR.

Phylogenomic databases

eggNOGiENOG4105VEJ. Bacteria.
COG1188. LUCA.
HOGENOMiHOG000216822.
InParanoidiP0ACG8.
KOiK04762.
OMAiRFYKTRT.
OrthoDBiEOG64NB4B.
PhylomeDBiP0ACG8.

Enzyme and pathway databases

BioCyciEcoCyc:G7743-MONOMER.
ECOL316407:JW3363-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ACG8.
PROiP0ACG8.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
InterProiIPR025708. HSP15.
IPR002942. S4_RNA-bd.
[Graphical view]
PfamiPF01479. S4. 1 hit.
[Graphical view]
PIRSFiPIRSF016821. HSP15. 1 hit.
SMARTiSM00363. S4. 1 hit.
[Graphical view]
PROSITEiPS50889. S4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "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.
  3. Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 1-9.
  4. "Hsp15: a ribosome-associated heat shock protein."
    Korber P., Stahl J.M., Nierhaus K.H., Bardwell J.C.A.
    EMBO J. 19:741-748(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Structure of Hsp15 reveals a novel RNA-binding motif."
    Staker B.L., Korber P., Bardwell J.C.A., Saper M.A.
    EMBO J. 19:749-757(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiHSLR_ECOLI
AccessioniPrimary (citable) accession number: P0ACG8
Secondary accession number(s): P45802, Q2M765
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: January 20, 2016
This is version 82 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.