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P43773 (HSLU_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP-dependent protease ATPase subunit HslU
Alternative name(s):
Unfoldase HslU
Gene names
Name:hslU
Ordered Locus Names:HI_0497
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length444 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. HAMAP-Rule MF_00249

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 By similarity.

Sequence similarities

Belongs to the ClpX chaperone family. HslU subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

hslVP437724EBI-1030296,EBI-1030290

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444ATP-dependent protease ATPase subunit HslU HAMAP-Rule MF_00249
PRO_0000160508

Regions

Nucleotide binding60 – 656ATP HAMAP-Rule MF_00249
Nucleotide binding306 – 3094ATP HAMAP-Rule MF_00249

Sites

Binding site181ATP; via amide nitrogen and carbonyl oxygen
Binding site2571ATP By similarity
Binding site3221ATP By similarity
Binding site3941ATP By similarity

Secondary structure

.................................................................... 444
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43773 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: C346EA478E4094CE

FASTA44449,372
        10         20         30         40         50         60 
MSEMTPREIV SELDQHIIGQ ADAKRAVAIA LRNRWRRMQL QEPLRHEVTP KNILMIGPTG 

        70         80         90        100        110        120 
VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDSAMKL VRQQEIAKNR 

       130        140        150        160        170        180 
ARAEDVAEER ILDALLPPAK NQWGEVENHD SHSSTRQAFR KKLREGQLDD KEIEIDVSAG 

       190        200        210        220        230        240 
VSMGVEIMAP PGMEEMTNQL QSLFQNLGSD KTKKRKMKIK DALKALIDDE AAKLINPEEL 

       250        260        270        280        290        300 
KQKAIDAVEQ NGIVFIDEID KICKKGEYSG ADVSREGVQR DLLPLVEGST VSTKHGMVKT 

       310        320        330        340        350        360 
DHILFIASGA FQVARPSDLI PELQGRLPIR VELTALSAAD FERILTEPHA SLTEQYKALM 

       370        380        390        400        410        420 
ATEGVNIAFT TDAVKKIAEA AFRVNEKTEN IGARRLHTVM ERLMDKISFS ASDMNGQTVN 

       430        440 
IDAAYVADAL GEVVENEDLS RFIL 

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]"Crystal and solution structures of an HslUV protease-chaperone complex."
Sousa M.C., Trame C.B., Tsuruta H., Wilbanks S.M., Reddy V.S., McKay D.B.
Cell 103:633-643(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.41 ANGSTROMS) OF 2-175 IN COMPLEX WITH HSLV AND ATP.
[3]"Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning."
Trame C.B., McKay D.B.
Acta Crystallogr. D 57:1079-1090(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ADP AND SULFATE.
[4]"Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome."
Kwon A.-R., Kessler B.M., Overkleeft H.S., McKay D.B.
J. Mol. Biol. 330:185-195(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-174 IN COMPLEX WITH HSLV; MAGNESIUM; ADP AND INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22154.1.
RefSeqNP_438655.1. NC_000907.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G3IX-ray3.41A/B/C/D/E/F/S/T/U/V/W/X1-444[»]
1G41X-ray2.30A1-444[»]
1IM2X-ray2.80A1-444[»]
1KYIX-ray3.10A/B/C/D/E/F/S/T/U/V/W/X1-444[»]
1OFHX-ray2.50A/B/C1-444[»]
1OFIX-ray3.20A/B/C1-444[»]
ProteinModelPortalP43773.
SMRP43773. Positions 1-444.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6175N.
IntActP43773. 1 interaction.
STRING71421.HI0497.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22154; AAC22154; HI_0497.
GeneID950614.
KEGGhin:HI0497.
PATRIC20189545. VBIHaeInf48452_0515.

Phylogenomic databases

eggNOGCOG1220.
KOK03667.
OMAKYGMIKT.
ProtClustDBPRK05201.

Family and domain databases

HAMAPMF_00249. HslU.
InterProIPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004491. HslU.
[Graphical view]
PANTHERPTHR11262:SF3. PTHR11262:SF3. 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...

Other

EvolutionaryTraceP43773.

Entry information

Entry nameHSLU_HAEIN
AccessionPrimary (citable) accession number: P43773
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families