SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q53080

- PSA1_RHOER

UniProt

Q53080 - PSA1_RHOER

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Proteasome subunit alpha 1

Gene
prcA1
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. protein binding Source: IntAct
  3. 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 1 (EC:3.4.25.1)
Alternative name(s):
20S proteasome alpha subunit 1
Proteasome core protein PrcA 1
Gene namesi
Name:prcA1
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 – 259259Proteasome subunit alpha 1UniRule annotationPRO_0000397128Add
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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
prcB1Q530792EBI-1037564,EBI-1037574

Protein-protein interaction databases

DIPiDIP-29143N.
IntActiQ53080. 1 interaction.

Structurei

Secondary structure

1
259
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2516
Beta strandi30 – 345
Beta strandi36 – 438
Beta strandi48 – 503
Beta strandi52 – 576
Beta strandi60 – 667
Helixi68 – 8821
Helixi91 – 933
Helixi96 – 11318
Beta strandi114 – 1163
Beta strandi120 – 1267
Beta strandi130 – 1323
Beta strandi137 – 1426
Turni143 – 1453
Beta strandi147 – 15913
Helixi160 – 17011
Helixi177 – 18812
Beta strandi206 – 2127
Beta strandi215 – 2173
Beta strandi220 – 2223
Helixi225 – 2295

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q5QX-ray2.60A/B/C/D/E/F/G1-259[»]
1Q5RX-ray3.10A/B/C/D/E/F/G8-259[»]
2H6JX-ray3.20A/B/C/D/E/F/G1-259[»]
ProteinModelPortaliQ53080.
SMRiQ53080. Positions 9-235.

Miscellaneous databases

EvolutionaryTraceiQ53080.

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.

Q53080-1 [UniParc]FASTAAdd to Basket

« Hide

MTMPYYASAE QIMRDRSELA RKGIARGRSV VVLTFRDGVL FVAENPSTAL    50
HKVSELYDRL GFAAVGKYNE FENLRRAGIV HADMRGYSYD RRDVTGRSLA 100
NAYAQTLGTI FTEQPKPYEV EICVAEVGRV GSPKAPQLYR ITYDGSIVDE 150
QHFVVMGGTT EPIATAMRES YRADLDLEAA VGIAVNALRQ GGAGEGEKRN 200
VDVASLEVAV LDQSRPRRAF RRIAGTALEQ LVPAEPAAAS ESAPEPKPDT 250
ETKPADTQD 259
Length:259
Mass (Da):28,312
Last modified:November 1, 1996 - v1
Checksum:iC1A97CACA2D77050
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U26421 Genomic DNA. Translation: AAC45741.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U26421 Genomic DNA. Translation: AAC45741.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q5Q X-ray 2.60 A/B/C/D/E/F/G 1-259 [» ]
1Q5R X-ray 3.10 A/B/C/D/E/F/G 8-259 [» ]
2H6J X-ray 3.20 A/B/C/D/E/F/G 1-259 [» ]
ProteinModelPortali Q53080.
SMRi Q53080. Positions 9-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29143N.
IntActi Q53080. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00997 .

Miscellaneous databases

EvolutionaryTracei Q53080.

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.
  3. "Crystal structures of the Rhodococcus proteasome with and without its pro-peptides: implications for the role of the pro-peptide in proteasome assembly."
    Kwon Y.D., Nagy I., Adams P.D., Baumeister W., Jap B.K.
    J. Mol. Biol. 335:233-245(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH BETA 1 SUBUNIT, PROTEASOME ASSEMBLY PROCESS.
  4. "Proteasome assembly triggers a switch required for active-site maturation."
    Witt S., Kwon Y.D., Sharon M., Felderer K., Beuttler M., Robinson C.V., Baumeister W., Jap B.K.
    Structure 14:1179-1188(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH BETA 1 SUBUNIT, PROTEASOME ASSEMBLY PROCESS.

Entry informationi

Entry nameiPSA1_RHOER
AccessioniPrimary (citable) accession number: Q53080
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 71 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

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi