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Q53084

- PSA2_RHOER

UniProt

Q53084 - PSA2_RHOER

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Protein
Proteasome subunit alpha 2
Gene
prcA2
Organism
Rhodococcus erythropolis (Arthrobacter picolinophilus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity.2 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.2 Publications

Enzyme regulationi

The formation of the proteasomal ATPase ARC-20S proteasome complex, likely via the docking of the C-termini of ARC into the intersubunit pockets in the alpha-rings, may trigger opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity By similarity.UniRule annotation

Kineticsi

The Vmax observed with the beta2-alpha1 proteasome subtype is 2.2-fold, 1.2-fold and 4-fold higher than that with the beta2-alpha2, beta1-alpha2 and beta1-alpha1 subtypes, respectively.

  1. KM=61.4 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha1 proteasome subtype)1 Publication
  2. KM=66.4 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha2 proteasome subtype)
  3. KM=71.2 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha2 proteasome subtype)
  4. KM=84.3 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha1 proteasome subtype)

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. proteasomal protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

UniPathwayiUPA00997.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha 2 (EC:3.4.25.1)
Alternative name(s):
20S proteasome alpha subunit 2
Proteasome core protein PrcA 2
Gene namesi
Name:prcA2
OrganismiRhodococcus erythropolis (Arthrobacter picolinophilus)
Taxonomic identifieri1833 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. proteasome core complex, alpha-subunit complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 255255Proteasome subunit alpha 2UniRule annotation
PRO_0000397129Add
BLAST

Post-translational modificationi

The N-terminus is blocked.UniRule annotation

Interactioni

Subunit structurei

The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. All four combinations of alpha- and beta-subunits (beta2-alpha1, beta2-alpha2, beta1-alpha2 and beta1-alpha1) yield fully assembled and proteolytically active proteasomes. The catalytic chamber with the active sites is on the inside of the barrel. Has probably a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is likely capped by the proteasome-associated ATPase, ARC.2 Publications

Structurei

3D structure databases

ProteinModelPortaliQ53084.
SMRiQ53084. Positions 9-238.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_00289_B. Proteasome_A_B.
InterProiIPR029055. Ntn_hydrolases_N.
IPR022296. Proteasome_asu_bac.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03691. 20S_bact_alpha. 1 hit.
PROSITEiPS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q53084-1 [UniParc]FASTAAdd to Basket

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MTMPYYASAE QIMRDRSELA RKGIARGRSV VVLTYRDGVL FVAENPSRAL    50
HKVSELYDRL GFAAVGKYNE FENLRRAGIV HADMRGYSYD RRDVTGRSLA 100
NAYAQTLGTI FTEQPKPYEV EICVAEIGRF GSSTPAQLYR ITYDGSIADE 150
QEFVVMGGTT EPIVTAMRES YQRDLDLESA VRLAVGALQK GGPAPAGTTE 200
AEPRTLDVSA LEVAVLDSNR PRRAFKRIAG SSLEEMLPTP AATEDAPPAN 250
GDAPS 255
Length:255
Mass (Da):27,859
Last modified:November 1, 1996 - v1
Checksum:iBCACDFEBDDB767B5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U26422 Genomic DNA. Translation: AAC45737.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U26422 Genomic DNA. Translation: AAC45737.1 .

3D structure databases

ProteinModelPortali Q53084.
SMRi Q53084. Positions 9-238.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00997 .

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
HAMAPi MF_00289_B. Proteasome_A_B.
InterProi IPR029055. Ntn_hydrolases_N.
IPR022296. Proteasome_asu_bac.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR03691. 20S_bact_alpha. 1 hit.
PROSITEi PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus."
    Tamura T., Nagy I., Lupas A., Lottspeich F., Cejka Z., Schoofs G., Tanaka K., de Mot R., Baumeister W.
    Curr. Biol. 5:766-774(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, BLOCKAGE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT.
    Strain: NI86/21.
  2. Cited for: SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS.
    Strain: NI86/21.

Entry informationi

Entry nameiPSA2_RHOER
AccessioniPrimary (citable) accession number: Q53084
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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