Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9V2V5 (PSA2_HALVD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha 2

EC=3.4.25.1
Alternative name(s):
20S proteasome alpha subunit 2
Proteasome core protein PsmA 2
Gene names
Name:psmA2
Synonyms:psmC
Ordered Locus Names:HVO_2923
OrganismHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) [Reference proteome] [HAMAP]
Taxonomic identifier309800 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta-alpha2 proteasome is able to cleave oligopeptides after Tyr and thus displays chymotrypsin-like activity. Ref.1 Ref.3

Catalytic activity

Cleavage of peptide bonds with very broad specificity. Ref.1 Ref.3

Enzyme regulation

The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers 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. HAMAP-Rule MF_00289

Subunit structure

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. H.volcanii produces at least 2 types of 20S proteasomes: an alpha1-beta proteasome and a proteasome containing all three subunits (alpha1, alpha2, and beta) that appears to be asymmetrical with homo-oligomeric alpha1 and alpha2 rings positioned on separate ends. 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 at one or both ends by the proteasome regulatory ATPase, PAN. Ref.1 Ref.3

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00289.

Induction

Up-regulated at mRNA and protein levels during transition from exponential to stationary phase. Ref.4

Disruption phenotype

Strains lacking psmA2 gene alone display relatively normal growth rate and overall cell yield. However, depletion of psmA1 and psmA2 together renders the cells inviable. Ref.6

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Proteasome subunit alpha 2 HAMAP-Rule MF_00289
PRO_0000124172

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9V2V5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7205A1A2B93E344E

FASTA24926,727
        10         20         30         40         50         60 
MNRNDKQAYD RGTSLFSPDG RIYQVEYARE AVKRGAPVLG VRTADGVVLA ALRSTPSELM 

        70         80         90        100        110        120 
EAESIEKLHK LDDALGAATA GHVADARKLV DFARTTAQRE HLRYGEPIGV ETLTKTITDN 

       130        140        150        160        170        180 
IQESTQSGGT RPYGASLLIG GVENGSGRLF ATDPSGTPQE WKAVAIGGHR EDVQAALEDG 

       190        200        210        220        230        240 
YAEDLSLEDG LALAVEALVA ADEEIESDEL NLVTVSEAGY EIVDEETIAE LFADATADDE 


SDETDEREE 

« Hide

References

« Hide 'large scale' references
[1]"Halophilic 20S proteasomes of the archaeon Haloferax volcanii: purification, characterization, and gene sequence analysis."
Wilson H.L., Aldrich H.C., Maupin-Furlow J.
J. Bacteriol. 181:5814-5824(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-31; 34-43 AND 89-98, BLOCKAGE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[2]"The complete genome sequence of Haloferax volcanii DS2, a model archaeon."
Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.
PLoS ONE 5:E9605-E9605(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2.
[3]"Subunit topology of two 20S proteasomes from Haloferax volcanii."
Kaczowka S.J., Maupin-Furlow J.A.
J. Bacteriol. 185:165-174(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, FUNCTION, CATALYTIC ACTIVITY.
[4]"Differential regulation of the PanA and PanB proteasome-activating nucleotidase and 20S proteasomal proteins of the haloarchaeon Haloferax volcanii."
Reuter C.J., Kaczowka S.J., Maupin-Furlow J.A.
J. Bacteriol. 186:7763-7772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[5]"Posttranslational modification of the 20S proteasomal proteins of the archaeon Haloferax volcanii."
Humbard M.A., Stevens S.M. Jr., Maupin-Furlow J.A.
J. Bacteriol. 188:7521-7530(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT MET-1.
[6]"Proteasomal components required for cell growth and stress responses in the haloarchaeon Haloferax volcanii."
Zhou G., Kowalczyk D., Humbard M.A., Rohatgi S., Maupin-Furlow J.A.
J. Bacteriol. 190:8096-8105(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF126261 Genomic DNA. Translation: AAD53405.1.
CP001956 Genomic DNA. Translation: ADE02793.1.
PIRT48679.
RefSeqYP_003536933.1. NC_013967.1.

3D structure databases

ProteinModelPortalQ9V2V5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE02793; ADE02793; HVO_2923.
GeneID8926453.
KEGGhvo:HVO_2923.

Phylogenomic databases

HOGENOMHOG000091085.
KOK03432.
OMARNDKQAY.

Enzyme and pathway databases

BioCycHVOL309800:GCOK-2929-MONOMER.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
HAMAPMF_00289_A. Proteasome_A_A.
InterProIPR029055. Ntn_hydrolases_N.
IPR019982. Proteasome_asu_arc.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSA2_HALVD
AccessionPrimary (citable) accession number: Q9V2V5
Secondary accession number(s): D4GXU2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries