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Q9Z617 (HSLU_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
Unfoldase HslU
Gene names
Name:hslU
Ordered Locus Names:BUsg_558
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. 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 By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00249.

Sequence similarities

Belongs to the ClpX chaperone family. HslU subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein unfolding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentHslUV protease complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

ATPase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

peptidase activity, acting on L-amino acid peptides

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443ATP-dependent protease ATPase subunit HslU HAMAP-Rule MF_00249
PRO_0000160487

Regions

Nucleotide binding60 – 656ATP By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q9Z617 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 914E269263FB8DB1

FASTA44350,030
        10         20         30         40         50         60 
MSEMTPPQIV SELNKFIIGQ EQAKKAVAIA LRNRWRRMQL NNELRHEITP KNILMIGPTG 

        70         80         90        100        110        120 
VGKTEIARRL AKLANSPFIK VEATKFTEVG YVGKEVDSII RDLTDAAIKM IRVKNIEKNK 

       130        140        150        160        170        180 
LRVEEIVEER ILDVLVPRPK NNWTENEKNE SLLNTLQVFR KKLREGILDE KEIEINVLAS 

       190        200        210        220        230        240 
TMGVEIMAPP GMEELTSQLQ SLFQNLGGHK KNTRRLKIKD AVLLLKEEEA AKLINQEEIK 

       250        260        270        280        290        300 
KEAINAVEQN GIVFVDEIDK ICKRRDSSGP DVSREGVQRD LLPLVEGCTV STKYGMVKTD 

       310        320        330        340        350        360 
HILFIASGAF QTSTPSDLIP ELQGRLPIKV ELQPLTINDF EKILTEPTAS ITAQYKALMK 

       370        380        390        400        410        420 
TEGVCINFTK EGIRNIAEAA WKVNESMENI GARRLHTILE KLMEDISFNA CDNVGKTIEI 

       430        440 
NSEYVGKHLD QLISNEDLGR FIL 

« Hide

References

« Hide 'large scale' references
[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.
[2]"Buchnera plasmid-associated trpEG probably originated from a chromosomal location between hslU and fpr."
Clark M.A., Baumann P., Moran M.A.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-443.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM68096.1.
AF108665 Genomic DNA. Translation: AAD19633.1.
RefSeqNP_660885.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ9Z617.
SMRQ9Z617. Positions 1-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg558.

Proteomic databases

PRIDEQ9Z617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM68096; AAM68096; BUsg_558.
GeneID1005633.
KEGGbas:BUsg558.
PATRIC21248002. VBIBucAph100086_0592.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1220.
KOK03667.
OMARLHTTIE.
OrthoDBEOG6NPM7G.
ProtClustDBPRK05201.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-590-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
HAMAPMF_00249. HslU.
InterProIPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004491. HslU.
IPR027417. P-loop_NTPase.
[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]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00390. hslU. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHSLU_BUCAP
AccessionPrimary (citable) accession number: Q9Z617
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 30, 2002
Last modified: April 16, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names