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D4GYZ1 (PSB_HALVD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Proteasome subunit beta

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit
Proteasome core protein PsmB
Gene names
Name:psmB
Ordered Locus Names:HVO_1562
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 length243 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activity but no trypsin-like activity. Ref.1

Catalytic activity

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

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. In vitro, the chymotrypsin-like activity of the alpha1-beta proteasome is potently inhibited by carbobenzoxyl-leucinyl-leucinyl-leucinal-H (MG132) and significantly by N-acetyl-leucinyl-leucinyl-norleucinal-H (calpain inhibitor I). Ref.1

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_02113.

Induction

Up-regulated at the mRNA level during transition from exponential to stationary phase. However, at the protein level, PsmB is expressed at a high and relatively constant level throughout growth. Ref.1 Ref.4

Disruption phenotype

Strains lacking psmB gene are inviable. Ref.6

Miscellaneous

H.volcanii proteasome requires high concentrations of salt, similar to the extracellular environment and cytoplasm of this organism, for complex stability and optimal activity.

Sequence similarities

Belongs to the peptidase T1B family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0-9.3 for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype). Ref.1

Temperature dependence:

Optimum temperature is 75 degrees Celsius for the Suc-LLVY-Amc hydrolyzing activity (with the alpha1-beta proteasome subtype).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 4949Removed in mature form; by autocatalysis HAMAP-Rule MF_02113
PRO_0000397605
Chain50 – 243194Proteasome subunit beta HAMAP-Rule MF_02113
PRO_0000397606

Sites

Active site501Nucleophile By similarity

Amino acid modifications

Modified residue1291Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
D4GYZ1 [UniParc].

Last modified May 18, 2010. Version 1.
Checksum: 6253E28ADDA40E61

FASTA24325,994
        10         20         30         40         50         60 
MRTPTHDEFS GRLDSLNGDR SNVFGPELGE FSNADRRADE LGDKETKTGT TTVGIKTEEG 

        70         80         90        100        110        120 
VVLATDMRAS MGYMVSSKDV QKVEEIHPTG ALTIAGSVSA AQSLISSLRA EVRLYEARRG 

       130        140        150        160        170        180 
EDMSMQALST LVGNFLRSGG FYVVQPILGG VDETGPHIYS IDPAGSILEE EYTVTGSGSQ 

       190        200        210        220        230        240 
YALGVLEQEF EDGLSIEEAK GVATKAIRSA VERDLASGNG INIAVVTEDG VDIQRHQNFE 


GLE 

« 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 50-79, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SALT REQUIREMENT, 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.
[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: PHOSPHORYLATION AT SER-129.
[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
AF126262 Genomic DNA. Translation: AAD53406.1.
CP001956 Genomic DNA. Translation: ADE03141.1.
PIRT48677.
RefSeqYP_003535609.1. NC_013967.1.

3D structure databases

ProteinModelPortalD4GYZ1.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPST01.002.

PTM databases

PhosSiteP0611175.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE03141; ADE03141; HVO_1562.
GeneID8923965.
KEGGhvo:HVO_1562.

Phylogenomic databases

HOGENOMHOG000091083.
KOK03433.
OMAMVDWLGT.

Enzyme and pathway databases

BioCycHVOL309800:GCOK-1565-MONOMER.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
HAMAPMF_02113_A. Proteasome_B_A.
InterProIPR029055. Ntn_hydrolases_N.
IPR019983. Pept_T1A_Psome_bsu_arc.
IPR000243. Pept_T1A_subB.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR03634. arc_protsome_B. 1 hit.
PROSITEPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSB_HALVD
AccessionPrimary (citable) accession number: D4GYZ1
Secondary accession number(s): Q9V2V4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 18, 2010
Last modified: June 11, 2014
This is version 28 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