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P0A7C0

- HSLV_ECO57

UniProt

P0A7C0 - HSLV_ECO57

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Protein
ATP-dependent protease subunit HslV
Gene
hslV, Z5479, ECs4859
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 By similarity.UniRule annotation

Catalytic activityi

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

Enzyme regulationi

Allosterically activated by HslU binding By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21 By similarity
Metal bindingi157 – 1571Sodium; via carbonyl oxygen By similarity
Metal bindingi160 – 1601Sodium; via carbonyl oxygen By similarity
Metal bindingi163 – 1631Sodium; via carbonyl oxygen By similarity

GO - Molecular functioni

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

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.

Names & Taxonomyi

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

Subcellular locationi

Cytoplasm By similarity 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 – 11Removed By similarity
Chaini2 – 176175ATP-dependent protease subunit HslVUniRule annotation
PRO_0000148106Add
BLAST

Expressioni

Inductioni

By heat shock By similarity.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 By similarity.

Protein-protein interaction databases

MINTiMINT-1218920.
STRINGi155864.Z5479.

Structurei

3D structure databases

ProteinModelPortaliP0A7C0.
SMRiP0A7C0. Positions 2-175.

Family & Domainsi

Sequence similaritiesi

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.

P0A7C0-1 [UniParc]FASTAAdd to Basket

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MTTIVSVRRN GHVVIAGDGQ ATLGNTVMKG NVKKVRRLYN DKVIAGFAGG    50
TADAFTLFEL FERKLEMHQG HLVKAAVELA KDWRTDRMLR KLEALLAVAD 100
ETASLIITGN GDVVQPENDL IAIGSGGPYA QAAARALLEN TELSAREIAE 150
KALDIAGDIC IYTNHFHTIE ELSYKA 176
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...

Protein-protein interaction databases

MINTi MINT-1218920.
STRINGi 155864.Z5479.

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: June 11, 2014
This is version 63 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

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