CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002909
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-dependent protease ATPase subunit HslU 
Protein Synonyms/Alias
 Heat shock protein HslU; Unfoldase HslU 
Gene Name
 hslU 
Gene Synonyms/Alias
 htpI; b3931; JW3902 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
15EIVSELDKHIIGQDNacetylation[1]
72EIARRLAKLANAPFIacetylation[1, 2]
80LANAPFIKVEATKFTacetylation[1]
94TEVGYVGKEVDSIIRacetylation[1]
109DLTDAAVKMVRVQAIacetylation[1]
118VRVQAIEKNRYRAEEacetylation[1, 2]
223LKIKDAMKLLIEEEAacetylation[1]
232LIEEEAAKLVNPEELacetylation[1]
260VFIDEIDKICKRGESacetylation[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]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 
Functional Description
 ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. 
Sequence Annotation
 NP_BIND 60 65 ATP.
 BINDING 18 18 ATP; via amide nitrogen and carbonyl
 BINDING 256 256 ATP.
 BINDING 321 321 ATP.
 BINDING 393 393 ATP.  
Keyword
 3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Nucleotide-binding; Reference proteome; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 443 AA 
Protein Sequence
MSEMTPREIV SELDKHIIGQ DNAKRSVAIA LRNRWRRMQL NEELRHEVTP KNILMIGPTG 60
VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDAAVKM VRVQAIEKNR 120
YRAEELAEER ILDVLIPPAK NNWGQTEQQQ EPSAARQAFR KKLREGQLDD KEIEIDLAAA 180
PMGVEIMAPP GMEEMTSQLQ SMFQNLGGQK QKARKLKIKD AMKLLIEEEA AKLVNPEELK 240
QDAIDAVEQH GIVFIDEIDK ICKRGESSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD 300
HILFIASGAF QIAKPSDLIP ELQGRLPIRV ELQALTTSDF ERILTEPNAS ITVQYKALMA 360
TEGVNIEFTD SGIKRIAEAA WQVNESTENI GARRLHTVLE RLMEEISYDA SDLSGQNITI 420
DADYVSKHLD ALVADEDLSR FIL 443 
Gene Ontology
 GO:0009376; C:HslUV protease complex; IEA:HAMAP.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0016887; F:ATPase activity; IEA:HAMAP.
 GO:0070011; F:peptidase activity, acting on L-amino acid peptides; IEA:InterPro.
 GO:0006200; P:ATP catabolic process; IEA:GOC.
 GO:0043335; P:protein unfolding; IEA:HAMAP.
 GO:0009408; P:response to heat; IEP:EcoliWiki. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR013093; ATPase_AAA-2.
 IPR003959; ATPase_AAA_core.
 IPR019489; Clp_ATPase_C.
 IPR004491; HslU.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00004; AAA
 PF07724; AAA_2
 PF10431; ClpB_D2-small 
SMART
 SM00382; AAA
 SM01086; ClpB_D2-small 
PROSITE
  
PRINTS