CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003354
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock protein 15 
Protein Synonyms/Alias
 HSP15 
Gene Name
 hslR 
Gene Synonyms/Alias
 yrfH; b3400; JW3363 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
2******MKEKPAVEVacetylation[1]
4****MKEKPAVEVRLacetylation[1]
13AVEVRLDKWLWAARFacetylation[1]
35REMIEGGKVHYNGQRacetylation[1]
94ETAESVEKREKMALAacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 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. 
Sequence Annotation
 DOMAIN 9 71 S4 RNA-binding.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; DNA-binding; Reference proteome; RNA-binding; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 133 AA 
Protein Sequence
MKEKPAVEVR LDKWLWAARF YKTRALAREM IEGGKVHYNG QRSKPSKIVE LNATLTLRQG 60
NDERTVIVKA ITEQRRPASE AALLYEETAE SVEKREKMAL ARKLNALTMP HPDRRPDKKE 120
RRDLLRFKHG DSE 133 
Gene Ontology
 GO:0003677; F:DNA binding; IDA:EcoCyc.
 GO:0043023; F:ribosomal large subunit binding; IDA:EcoCyc.
 GO:0003727; F:single-stranded RNA binding; IDA:EcoCyc.
 GO:0034605; P:cellular response to heat; IEP:EcoCyc. 
Interpro
 IPR025708; HSP15.
 IPR002942; S4_RNA-bd. 
Pfam
 PF01479; S4 
SMART
 SM00363; S4 
PROSITE
 PS50889; S4 
PRINTS