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P0A7C0

- HSLV_ECO57

UniProt

P0A7C0 - HSLV_ECO57

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Protein

ATP-dependent protease subunit HslV

Gene

hslV

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.UniRule annotation

Catalytic activityi

ATP-dependent cleavage of peptide bonds with broad specificity.UniRule annotation

Enzyme regulationi

Allosterically activated by HslU binding.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21UniRule annotation
Metal bindingi157 – 1571Sodium; via carbonyl oxygenUniRule annotation
Metal bindingi160 – 1601Sodium; via carbonyl oxygenUniRule annotation
Metal bindingi163 – 1631Sodium; via carbonyl oxygenUniRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
  2. response to stress Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Stress response

Keywords - Ligandi

Metal-binding, Sodium

Enzyme and pathway databases

BioCyciECOL386585:GJFA-4849-MONOMER.
ECOO157:HSLV-MONOMER.

Protein family/group databases

MEROPSiT01.006.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent protease subunit HslVUniRule annotation (EC:3.4.25.2UniRule annotation)
Alternative name(s):
Heat shock protein HslVUniRule annotation
Gene namesi
Name:hslVUniRule annotation
Ordered Locus Names:Z5479, ECs4859
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. HslUV protease complex Source: UniProtKB-HAMAP
  2. proteasome core complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 176175ATP-dependent protease subunit HslVPRO_0000148106Add
BLAST

Expressioni

Inductioni

By heat shock.UniRule annotation

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.UniRule annotation

Protein-protein interaction databases

MINTiMINT-1218920.
STRINGi155864.Z5479.

Structurei

3D structure databases

ProteinModelPortaliP0A7C0.
SMRiP0A7C0. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family. HslV subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG5405.
HOGENOMiHOG000064533.
KOiK01419.
OMAiRLYHGKV.
OrthoDBiEOG6ND0PJ.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00248. HslV.
InterProiIPR022281. ATP-dep_Prtase_HsIV_su.
IPR029055. Ntn_hydrolases_N.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03692. ATP_dep_HslV. 1 hit.
PROSITEiPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7C0 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTIVSVRRN GHVVIAGDGQ ATLGNTVMKG NVKKVRRLYN DKVIAGFAGG
60 70 80 90 100
TADAFTLFEL FERKLEMHQG HLVKAAVELA KDWRTDRMLR KLEALLAVAD
110 120 130 140 150
ETASLIITGN GDVVQPENDL IAIGSGGPYA QAAARALLEN TELSAREIAE
160 170
KALDIAGDIC IYTNHFHTIE ELSYKA
Length:176
Mass (Da):19,093
Last modified:January 23, 2007 - v2
Checksum:i3B35E01F51486965
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG59127.1.
BA000007 Genomic DNA. Translation: BAB38282.1.
PIRiC86083.
C91236.
RefSeqiNP_290563.1. NC_002655.2.
NP_312886.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG59127; AAG59127; Z5479.
BAB38282; BAB38282; BAB38282.
GeneIDi915032.
960205.
KEGGiece:Z5479.
ecs:ECs4859.
PATRICi18359379. VBIEscCol44059_4839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG59127.1 .
BA000007 Genomic DNA. Translation: BAB38282.1 .
PIRi C86083.
C91236.
RefSeqi NP_290563.1. NC_002655.2.
NP_312886.1. NC_002695.1.

3D structure databases

ProteinModelPortali P0A7C0.
SMRi P0A7C0. Positions 2-175.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1218920.
STRINGi 155864.Z5479.

Protein family/group databases

MEROPSi T01.006.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG59127 ; AAG59127 ; Z5479 .
BAB38282 ; BAB38282 ; BAB38282 .
GeneIDi 915032.
960205.
KEGGi ece:Z5479.
ecs:ECs4859.
PATRICi 18359379. VBIEscCol44059_4839.

Phylogenomic databases

eggNOGi COG5405.
HOGENOMi HOG000064533.
KOi K01419.
OMAi RLYHGKV.
OrthoDBi EOG6ND0PJ.

Enzyme and pathway databases

BioCyci ECOL386585:GJFA-4849-MONOMER.
ECOO157:HSLV-MONOMER.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
HAMAPi MF_00248. HslV.
InterProi IPR022281. ATP-dep_Prtase_HsIV_su.
IPR029055. Ntn_hydrolases_N.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR03692. ATP_dep_HslV. 1 hit.
PROSITEi PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiHSLV_ECO57
AccessioniPrimary (citable) accession number: P0A7C0
Secondary accession number(s): P31059, P97542
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3