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Protein

ATP-dependent protease ATPase subunit HslU

Gene

hslU

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

Functioni

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.7 Publications

Kineticsi

Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.

  1. KM=0.31 mM for ATP (in the absence of HslV)2 Publications
  2. KM=0.28 mM for ATP (in the presence of HslV)2 Publications
  3. KM=5.2 µM for Arc-MYL-st11 (at 37 degrees Celsius)2 Publications
  1. Vmax=57 pmol/min/mg enzyme (in the absence of HslV)2 Publications
  2. Vmax=213 pmol/min/mg enzyme (in the presence of HslV)2 Publications

Temperature dependencei

Optimum temperature is 55 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei18ATP; via amide nitrogen and carbonyl oxygen1
Binding sitei256ATP1
Binding sitei321ATP1
Binding sitei393ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi60 – 65ATP6

GO - Molecular functioni

  • ATPase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-HAMAP
  • peptidase activity, acting on L-amino acid peptides Source: InterPro

GO - Biological processi

  • protein unfolding Source: EcoCyc
  • response to heat Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11881-MONOMER.
ECOL316407:JW3902-MONOMER.
MetaCyc:EG11881-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent protease ATPase subunit HslU
Alternative name(s):
Heat shock protein HslU
Unfoldase HslU
Gene namesi
Name:hslU
Synonyms:htpI
Ordered Locus Names:b3931, JW3902
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11881. hslU.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • HslUV protease complex Source: UniProtKB-HAMAP
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi63K → T: Can neither bind nor hydrolyze ATP. Do not form multimers, but stays as monomer. 1 Publication1
Mutagenesisi80K → T: Some effect on protease activity. 1 Publication1
Mutagenesisi88E → Q: Severly reduced protease activity. 1 Publication1
Mutagenesisi91Y → G: Partial loss of protease activity. 1 Publication1
Mutagenesisi92V → G: Partial loss of protease activity. 1 Publication1
Mutagenesisi93G → A: Almost no protease or ATP hydrolysis activity. 1 Publication1
Mutagenesisi95E → W: Partial loss of protease activity. 1 Publication1
Mutagenesisi262C → V: No effect on ATP hydrolysis. Can support HslV-mediated proteolysis at wild-type levels. 1 Publication1
Mutagenesisi266E → Q: No effect. 1 Publication1
Mutagenesisi286E → Q: Reduced protease activity. 1 Publication1
Mutagenesisi288C → V: No ATP hydrolysis activity. Binds ATP with lower affinity than wild-type. Can support HslV-mediated proteolysis to some extent. 1 Publication1
Mutagenesisi312I → W: No effect. 1 Publication1
Mutagenesisi321E → Q: Complete loss of activity. 1 Publication1
Mutagenesisi325R → E: Complete loss of activity. Forms wild-type complexes with HslV and is able to bind ATP. 1 Publication1
Mutagenesisi385E → K: No effect. 1 Publication1
Mutagenesisi393R → A: Complete loss of activity. 1 Publication1
Mutagenesisi436E → K: Partial loss of protease activity; when associated with K-437. 1
Mutagenesisi437D → K: Partial loss of protease activity; when associated with K-436. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001605001 – 443ATP-dependent protease ATPase subunit HslUAdd BLAST443

Proteomic databases

EPDiP0A6H5.
PaxDbiP0A6H5.
PRIDEiP0A6H5.

2D gel databases

SWISS-2DPAGEP0A6H5.

Expressioni

Inductioni

By heat shock.1 Publication

Interactioni

Subunit structurei

A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-369317,EBI-369317
hslVP0A7B86EBI-369317,EBI-552265
sulAP0AFZ55EBI-369317,EBI-2012039

Protein-protein interaction databases

BioGridi4261787. 209 interactors.
DIPiDIP-31855N.
IntActiP0A6H5. 46 interactors.
STRINGi511145.b3931.

Structurei

Secondary structure

1443
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 14Combined sources9
Helixi21 – 38Combined sources18
Helixi42 – 47Combined sources6
Beta strandi53 – 56Combined sources4
Helixi63 – 71Combined sources9
Turni72 – 75Combined sources4
Beta strandi78 – 82Combined sources5
Helixi83 – 90Combined sources8
Helixi98 – 113Combined sources16
Turni114 – 117Combined sources4
Helixi118 – 121Combined sources4
Beta strandi124 – 126Combined sources3
Helixi127 – 132Combined sources6
Turni133 – 135Combined sources3
Helixi147 – 149Combined sources3
Turni150 – 154Combined sources5
Helixi155 – 161Combined sources7
Beta strandi171 – 173Combined sources3
Beta strandi214 – 216Combined sources3
Helixi224 – 232Combined sources9
Helixi237 – 240Combined sources4
Helixi242 – 250Combined sources9
Beta strandi252 – 256Combined sources5
Helixi258 – 261Combined sources4
Helixi269 – 286Combined sources18
Beta strandi289 – 292Combined sources4
Beta strandi295 – 298Combined sources4
Helixi299 – 301Combined sources3
Beta strandi303 – 308Combined sources6
Beta strandi311 – 313Combined sources3
Helixi315 – 317Combined sources3
Helixi320 – 324Combined sources5
Beta strandi328 – 331Combined sources4
Helixi337 – 345Combined sources9
Helixi351 – 361Combined sources11
Beta strandi365 – 368Combined sources4
Helixi370 – 386Combined sources17
Helixi393 – 409Combined sources17
Helixi410 – 413Combined sources4
Beta strandi417 – 420Combined sources4
Helixi422 – 434Combined sources13
Helixi436 – 442Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DO0X-ray3.00A/B/C/D/E/F2-443[»]
1DO2X-ray4.00A/B/C/D2-443[»]
1E94X-ray2.80E/F2-443[»]
1G4AX-ray3.00E/F1-443[»]
1G4BX-ray7.00E/F/K/L1-443[»]
1HQYX-ray2.80E/F2-443[»]
1HT1X-ray2.80E/F/G/I2-443[»]
1HT2X-ray2.80E/F/G/H2-443[»]
1YYFX-ray4.16A/B1-443[»]
DisProtiDP00100.
ProteinModelPortaliP0A6H5.
SMRiP0A6H5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6H5.

Family & Domainsi

Sequence similaritiesi

Belongs to the ClpX chaperone family. HslU subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105C4N. Bacteria.
COG1220. LUCA.
HOGENOMiHOG000010036.
InParanoidiP0A6H5.
KOiK03667.
OMAiAKIMELP.
PhylomeDBiP0A6H5.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00249. HslU. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004491. HslU.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11262:SF3. PTHR11262:SF3. 2 hits.
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00390. hslU. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6H5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEMTPREIV SELDKHIIGQ DNAKRSVAIA LRNRWRRMQL NEELRHEVTP
60 70 80 90 100
KNILMIGPTG VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII
110 120 130 140 150
RDLTDAAVKM VRVQAIEKNR YRAEELAEER ILDVLIPPAK NNWGQTEQQQ
160 170 180 190 200
EPSAARQAFR KKLREGQLDD KEIEIDLAAA PMGVEIMAPP GMEEMTSQLQ
210 220 230 240 250
SMFQNLGGQK QKARKLKIKD AMKLLIEEEA AKLVNPEELK QDAIDAVEQH
260 270 280 290 300
GIVFIDEIDK ICKRGESSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD
310 320 330 340 350
HILFIASGAF QIAKPSDLIP ELQGRLPIRV ELQALTTSDF ERILTEPNAS
360 370 380 390 400
ITVQYKALMA TEGVNIEFTD SGIKRIAEAA WQVNESTENI GARRLHTVLE
410 420 430 440
RLMEEISYDA SDLSGQNITI DADYVSKHLD ALVADEDLSR FIL
Length:443
Mass (Da):49,594
Last modified:March 29, 2005 - v1
Checksum:iD2188639EA9AEF4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03063.1.
U00096 Genomic DNA. Translation: AAC76913.1.
AP009048 Genomic DNA. Translation: BAE77379.1.
PIRiJT0761.
RefSeqiNP_418366.1. NC_000913.3.
WP_001293341.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76913; AAC76913; b3931.
BAE77379; BAE77379; BAE77379.
GeneIDi948430.
KEGGiecj:JW3902.
eco:b3931.
PATRICi32123377. VBIEscCol129921_4049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03063.1.
U00096 Genomic DNA. Translation: AAC76913.1.
AP009048 Genomic DNA. Translation: BAE77379.1.
PIRiJT0761.
RefSeqiNP_418366.1. NC_000913.3.
WP_001293341.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DO0X-ray3.00A/B/C/D/E/F2-443[»]
1DO2X-ray4.00A/B/C/D2-443[»]
1E94X-ray2.80E/F2-443[»]
1G4AX-ray3.00E/F1-443[»]
1G4BX-ray7.00E/F/K/L1-443[»]
1HQYX-ray2.80E/F2-443[»]
1HT1X-ray2.80E/F/G/I2-443[»]
1HT2X-ray2.80E/F/G/H2-443[»]
1YYFX-ray4.16A/B1-443[»]
DisProtiDP00100.
ProteinModelPortaliP0A6H5.
SMRiP0A6H5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261787. 209 interactors.
DIPiDIP-31855N.
IntActiP0A6H5. 46 interactors.
STRINGi511145.b3931.

2D gel databases

SWISS-2DPAGEP0A6H5.

Proteomic databases

EPDiP0A6H5.
PaxDbiP0A6H5.
PRIDEiP0A6H5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76913; AAC76913; b3931.
BAE77379; BAE77379; BAE77379.
GeneIDi948430.
KEGGiecj:JW3902.
eco:b3931.
PATRICi32123377. VBIEscCol129921_4049.

Organism-specific databases

EchoBASEiEB1827.
EcoGeneiEG11881. hslU.

Phylogenomic databases

eggNOGiENOG4105C4N. Bacteria.
COG1220. LUCA.
HOGENOMiHOG000010036.
InParanoidiP0A6H5.
KOiK03667.
OMAiAKIMELP.
PhylomeDBiP0A6H5.

Enzyme and pathway databases

BioCyciEcoCyc:EG11881-MONOMER.
ECOL316407:JW3902-MONOMER.
MetaCyc:EG11881-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6H5.
PROiP0A6H5.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00249. HslU. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004491. HslU.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11262:SF3. PTHR11262:SF3. 2 hits.
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00390. hslU. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHSLU_ECOLI
AccessioniPrimary (citable) accession number: P0A6H5
Secondary accession number(s): P32168, Q2M8M7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: November 2, 2016
This is version 108 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, 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.