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P0A7C0 (HSLV_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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 subunit HslV

EC=3.4.25.2
Alternative name(s):
Heat shock protein HslV
Gene names
Name:hslV
Ordered Locus Names:Z5479, ECs4859
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery By similarity. HAMAP-Rule MF_00248

Catalytic activity

ATP-dependent cleavage of peptide bonds with broad specificity. HAMAP-Rule MF_00248

Enzyme regulation

Allosterically activated by HslU binding By similarity. HAMAP-Rule MF_00248

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_00248.

Induction

By heat shock By similarity. HAMAP-Rule MF_00248

Sequence similarities

Belongs to the peptidase T1B family. HslV subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 176175ATP-dependent protease subunit HslV HAMAP-Rule MF_00248
PRO_0000148106

Sites

Active site21 By similarity
Metal binding1571Sodium; via carbonyl oxygen By similarity
Metal binding1601Sodium; via carbonyl oxygen By similarity
Metal binding1631Sodium; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A7C0 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3B35E01F51486965

FASTA17619,093
        10         20         30         40         50         60 
MTTIVSVRRN GHVVIAGDGQ ATLGNTVMKG NVKKVRRLYN DKVIAGFAGG TADAFTLFEL 

        70         80         90        100        110        120 
FERKLEMHQG HLVKAAVELA KDWRTDRMLR KLEALLAVAD ETASLIITGN GDVVQPENDL 

       130        140        150        160        170 
IAIGSGGPYA QAAARALLEN TELSAREIAE KALDIAGDIC IYTNHFHTIE ELSYKA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG59127.1.
BA000007 Genomic DNA. Translation: BAB38282.1.
PIRC86083.
C91236.
RefSeqNP_290563.1. NC_002655.2.
NP_312886.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A7C0.
SMRP0A7C0. Positions 2-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1218920.
STRING155864.Z5479.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG59127; AAG59127; Z5479.
BAB38282; BAB38282; BAB38282.
GeneID915032.
960205.
KEGGece:Z5479.
ecs:ECs4859.
PATRIC18359379. VBIEscCol44059_4839.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG5405.
HOGENOMHOG000064533.
KOK01419.
OMAELCIYTN.
OrthoDBEOG6ND0PJ.
ProtClustDBPRK05456.

Enzyme and pathway databases

BioCycECOL386585:GJFA-4849-MONOMER.
ECOO157:HSLV-MONOMER.

Family and domain databases

HAMAPMF_00248. HslV.
InterProIPR022281. ATP-dep_Prtase_HsIV_su.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
TIGRFAMsTIGR03692. ATP_dep_HslV. 1 hit.
PROSITEPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHSLV_ECO57
AccessionPrimary (citable) accession number: P0A7C0
Secondary accession number(s): P31059, P97542
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 61 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

Peptidase families

Classification of peptidase families and list of entries