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P0A6H5 (HSLU_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent protease ATPase subunit HslU
Alternative name(s):
Heat shock protein HslU
Unfoldase HslU
Gene names
Name:hslU
Synonyms:htpI
Ordered Locus Names:b3931, JW3902
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14

Subunit structure

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.

Subcellular location

Cytoplasm HAMAP MF_00249.

Induction

By heat shock. Ref.1

Sequence similarities

Belongs to the ClpX chaperone family. HslU subfamily.

Biophysicochemical properties

Kinetic parameters:

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

KM=0.31 mM for ATP (in the absence of HslV) Ref.6 Ref.14

KM=0.28 mM for ATP (in the presence of HslV)

KM=5.2 µM for Arc-MYL-st11 (at 37 degrees Celsius)

Vmax=57 pmol/min/mg enzyme (in the absence of HslV)

Vmax=213 pmol/min/mg enzyme (in the presence of HslV)

Temperature dependence:

Optimum temperature is 55 degrees Celsius.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-369317,EBI-369317
hslVP0A7B87EBI-369317,EBI-552265

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443ATP-dependent protease ATPase subunit HslU HAMAP MF_00249
PRO_0000160500

Regions

Nucleotide binding60 – 656ATP HAMAP MF_00249

Sites

Binding site181ATP; via amide nitrogen and carbonyl oxygen
Binding site2561ATP
Binding site3211ATP
Binding site3931ATP

Experimental info

Mutagenesis631K → T: Can neither bind nor hydrolyze ATP. Do not form multimers, but stays as monomer. Ref.5
Mutagenesis801K → T: Some effect on protease activity. Ref.17
Mutagenesis881E → Q: Severly reduced protease activity. Ref.17
Mutagenesis911Y → G: Partial loss of protease activity. Ref.17
Mutagenesis921V → G: Partial loss of protease activity. Ref.17
Mutagenesis931G → A: Almost no protease or ATP hydrolysis activity. Ref.17
Mutagenesis951E → W: Partial loss of protease activity. Ref.17
Mutagenesis2621C → V: No effect on ATP hydrolysis. Can support HslV-mediated proteolysis at wild-type levels. Ref.11
Mutagenesis2661E → Q: No effect. Ref.17
Mutagenesis2861E → Q: Reduced protease activity. Ref.17
Mutagenesis2881C → V: No ATP hydrolysis activity. Binds ATP with lower affinity than wild-type. Can support HslV-mediated proteolysis to some extent. Ref.11
Mutagenesis3121I → W: No effect. Ref.17
Mutagenesis3211E → Q: Complete loss of activity. Ref.17
Mutagenesis3251R → E: Complete loss of activity. Forms wild-type complexes with HslV and is able to bind ATP. Ref.17
Mutagenesis3851E → K: No effect. Ref.17
Mutagenesis3931R → A: Complete loss of activity. Ref.17
Mutagenesis4361E → K: Partial loss of protease activity; when associated with K-437.
Mutagenesis4371D → K: Partial loss of protease activity; when associated with K-436.

Secondary structure

........................................................................ 443
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6H5 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: D2188639EA9AEF4C

FASTA44349,594
        10         20         30         40         50         60 
MSEMTPREIV SELDKHIIGQ DNAKRSVAIA LRNRWRRMQL NEELRHEVTP KNILMIGPTG 

        70         80         90        100        110        120 
VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDAAVKM VRVQAIEKNR 

       130        140        150        160        170        180 
YRAEELAEER ILDVLIPPAK NNWGQTEQQQ EPSAARQAFR KKLREGQLDD KEIEIDLAAA 

       190        200        210        220        230        240 
PMGVEIMAPP GMEEMTSQLQ SMFQNLGGQK QKARKLKIKD AMKLLIEEEA AKLVNPEELK 

       250        260        270        280        290        300 
QDAIDAVEQH GIVFIDEIDK ICKRGESSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD 

       310        320        330        340        350        360 
HILFIASGAF QIAKPSDLIP ELQGRLPIRV ELQALTTSDF ERILTEPNAS ITVQYKALMA 

       370        380        390        400        410        420 
TEGVNIEFTD SGIKRIAEAA WQVNESTENI GARRLHTVLE RLMEEISYDA SDLSGQNITI 

       430        440 
DADYVSKHLD ALVADEDLSR FIL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli."
Chuang S.E., Burland V., Plunkett G. III, Daniels D.L., Blattner F.R.
Gene 134:1-6(1993) [PubMed: 8244018] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: K12 / MG1655 / ATCC 47076.
[2]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed: 8346018] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli."
Shin D.H., Yoo S.J., Shim Y.K., Seol J.H., Kang M.S., Chung C.H.
FEBS Lett. 398:151-154(1996) [PubMed: 8977096] [Abstract]
Cited for: MUTAGENESIS OF LYS-63.
[6]"Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli."
Yoo S.J., Seol J.H., Shin D.H., Rohrwild M., Kang M.-S., Tanaka K., Goldberg A.L., Chung C.H.
J. Biol. Chem. 271:14035-14040(1996) [PubMed: 8662828] [Abstract]
Cited for: FUNCTION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome."
Rohrwild M., Coux O., Huang H.-C., Moerschell R.P., Yoo S.J., Seol J.H., Chung C.H., Goldberg A.L.
Proc. Natl. Acad. Sci. U.S.A. 93:5808-5813(1996) [PubMed: 8650174] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[8]"ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli."
Yoo S.J., Seol J.H., Seong I.S., Kang M.-S., Chung C.H.
Biochem. Biophys. Res. Commun. 238:581-585(1997) [PubMed: 9299555] [Abstract]
Cited for: EFFECTS OF ATP BINDING ON COMPLEX FORMATION.
[9]"The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase."
Seol J.H., Yoo S.J., Shin D.H., Shim Y.K., Kang M.-S., Goldberg A.L., Chung C.H.
Eur. J. Biochem. 247:1143-1150(1997) [PubMed: 9288941] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
[10]"Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli."
Kanemori M., Nishihara K., Yanagi H., Yura T.
J. Bacteriol. 179:7219-7225(1997) [PubMed: 9393683] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[11]"Effects of the cys mutations on structure and function of the ATP-dependent HslVU protease in Escherichia coli. The Cys287 to Val mutation in HslU uncouples the ATP-dependent proteolysis by HslvU from ATP hydrolysis."
Yoo S.J., Kim H.H., Shin D.H., Lee C.S., Seong I.S., Seol J.H., Shimbara N., Tanaka K., Chung C.H.
J. Biol. Chem. 273:22929-22935(1998) [PubMed: 9722513] [Abstract]
Cited for: MUTAGENESIS OF CYS-262 AND CYS-288.
[12]"ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli."
Seong I.S., Oh J.Y., Yoo S.J., Seol J.H., Chung C.H.
FEBS Lett. 456:211-214(1999) [PubMed: 10452560] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[13]"Marked instability of the sigma(32) heat shock transcription factor at high temperature. Implications for heat shock regulation."
Kanemori M., Yanagi H., Yura T.
J. Biol. Chem. 274:22002-22007(1999) [PubMed: 10419524] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION.
[14]"Nucleotide-dependent substrate recognition by the AAA+ HslUV protease."
Burton R.E., Baker T.A., Sauer R.T.
Nat. Struct. Mol. Biol. 12:245-251(2005) [PubMed: 15696175] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[15]"HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis."
Lee J.W., Park E., Jeong M.S., Jeon Y.J., Eom S.H., Seol J.H., Chung C.H.
J. Biol. Chem. 284:33475-33484(2009) [PubMed: 19801685] [Abstract]
Cited for: REACTION MECHANISM.
[16]"The structures of HslU and the ATP-dependent protease HslU-HslV."
Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R.
Nature 403:800-805(2000) [PubMed: 10693812] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF COMPLEXES WITH ATP AND HSLV.
[17]"Mutational studies on HslU and its docking mode with HslV."
Song H.K., Hartmann C., Ramachandran R., Bochtler M., Behrendt R., Moroder L., Huber R.
Proc. Natl. Acad. Sci. U.S.A. 97:14103-14108(2000) [PubMed: 11114186] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-176 OF APOENZYME AND IN COMPLEXES WITH HSLV AND ATP, MUTAGENESIS OF LYS-80; GLU-88; TYR-91; VAL-92; GLY-93; GLU-95; GLU-266; GLU-286; ILE-312; GLU-321; ARG-325; GLU-385 AND ARG-393.
[18]"Nucleotide-dependent conformational changes in a protease-associated ATPase HslU."
Wang J., Song J.J., Seong I.S., Franklin M.C., Kamtekar S., Eom S.H., Chung C.H.
Structure 9:1107-1116(2001) [PubMed: 11709174] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-443 IN COMPLEX WITH ADP.
[19]"Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects."
Wang J., Rho S.H., Park H.H., Eom S.H.
Acta Crystallogr. D 61:932-941(2005) [PubMed: 15983416] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.16 ANGSTROMS) IN COMPLEX WITH B.SUBTILIS HSLV AND ADP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19201 Genomic DNA. Translation: AAB03063.1.
U00096 Genomic DNA. Translation: AAC76913.1.
AP009048 Genomic DNA. Translation: BAE77379.1.
PIRJT0761.
RefSeqNP_418366.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0A6H5.
SMRP0A6H5. Positions 1-443.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31855N.
IntActP0A6H5. 48 interactions.

2D gel databases

SWISS-2DPAGEP0A6H5.
ECO2DBASED048.5. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000003987; EBESCP00000003987; EBESCG00000003262.
EBESCT00000018172; EBESCP00000017463; EBESCG00000017227.
GeneID948430.
GenomeReviewsGene locus JW3902 in contig AP009048_GR.
Gene locus b3931 in contig U00096_GR.
KEGGecj:JW3902.
eco:b3931.
PATRIC32123377. VBIEscCol129921_4049.

Organism-specific databases

EchoBASEEB1827.
EcoGeneEG11881. hslU.

Phylogenomic databases

eggNOGCOG1220.
GeneTreeEBGT00050000010205.
HOGENOMHBG745965.
OMAEASKFTE.
PhylomeDBP0A6H5.
ProtClustDBPRK05201.

Enzyme and pathway databases

BioCycEcoCyc:EG11881-MONOMER.

Gene expression databases

GenevestigatorP0A6H5.

Family and domain databases

HAMAPMF_00249. HslU.
[Tree]
InterProIPR003593. ATPase_AAA+_core.
IPR013093. ATPase_AAA-2.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004491. HslU.
[Graphical view]
KOK03667.
PANTHERPTHR11262:SF3. HslU. 1 hit.
PfamPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
TIGRFAMsTIGR00390. HslU. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHSLU_ECOLI
AccessionPrimary (citable) accession number: P0A6H5
Secondary accession number(s): P32168, Q2M8M7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families