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Protein

Proteasome subunit alpha 1

Gene

prcA1

Organism
Rhodococcus erythropolis (Arthrobacter picolinophilus)
Status
Reviewed-Annotation score: 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.UniRule annotation2 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.UniRule annotation2 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.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)1 Publication
  3. KM=71.2 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha2 proteasome subtype)1 Publication
  4. KM=84.3 µM for Suc-Leu-Leu-Val-Tyr-AMC (with the beta1-alpha1 proteasome subtype)1 Publication

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. modification-dependent protein catabolic process Source: UniProtKB-HAMAP
  2. 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 1UniRule annotation (EC:3.4.25.1UniRule annotation)
Alternative name(s):
20S proteasome alpha subunit 1UniRule annotation
Proteasome core protein PrcA 1UniRule annotation
Gene namesi
Name:prcA1UniRule annotation
OrganismiRhodococcus erythropolis (Arthrobacter picolinophilus)
Taxonomic identifieri1833 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Subcellular locationi

Cytoplasm 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 1PRO_0000397128Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

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 – 2516Combined sources
Beta strandi30 – 345Combined sources
Beta strandi36 – 438Combined sources
Beta strandi48 – 503Combined sources
Beta strandi52 – 576Combined sources
Beta strandi60 – 667Combined sources
Helixi68 – 8821Combined sources
Helixi91 – 933Combined sources
Helixi96 – 11318Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi137 – 1426Combined sources
Turni143 – 1453Combined sources
Beta strandi147 – 15913Combined sources
Helixi160 – 17011Combined sources
Helixi177 – 18812Combined sources
Beta strandi206 – 2127Combined sources
Beta strandi215 – 2173Combined sources
Beta strandi220 – 2223Combined sources
Helixi225 – 2295Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53080.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.UniRule annotation

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

        10         20         30         40         50
MTMPYYASAE QIMRDRSELA RKGIARGRSV VVLTFRDGVL FVAENPSTAL
60 70 80 90 100
HKVSELYDRL GFAAVGKYNE FENLRRAGIV HADMRGYSYD RRDVTGRSLA
110 120 130 140 150
NAYAQTLGTI FTEQPKPYEV EICVAEVGRV GSPKAPQLYR ITYDGSIVDE
160 170 180 190 200
QHFVVMGGTT EPIATAMRES YRADLDLEAA VGIAVNALRQ GGAGEGEKRN
210 220 230 240 250
VDVASLEVAV LDQSRPRRAF RRIAGTALEQ LVPAEPAAAS ESAPEPKPDT

ETKPADTQD
Length:259
Mass (Da):28,312
Last modified:November 1, 1996 - v1
Checksum:iC1A97CACA2D77050
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26421 Genomic DNA. Translation: AAC45741.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26421 Genomic DNA. Translation: AAC45741.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29143N.
IntActiQ53080. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00997.

Miscellaneous databases

EvolutionaryTraceiQ53080.

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]
ProtoNetiSearch...

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(1994) [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(2003) [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(2005) [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: February 4, 2015
This is version 76 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.