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Protein

Proteasome subunit beta 2

Gene

psmB2

Organism
Hyperthermus butylicus (strain DSM 5456 / JCM 9403)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.UniRule annotation

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.UniRule annotation

Enzyme regulationi

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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei16 – 161NucleophileUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciHBUT415426:GC56-1567-MONOMER.

Protein family/group databases

MEROPSiT01.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta 2UniRule annotation (EC:3.4.25.1UniRule annotation)
Alternative name(s):
20S proteasome beta subunit 2UniRule annotation
Proteasome core protein PsmB 2UniRule annotation
Gene namesi
Name:psmB2UniRule annotation
Ordered Locus Names:Hbut_1567
OrganismiHyperthermus butylicus (strain DSM 5456 / JCM 9403)
Taxonomic identifieri415426 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus
ProteomesiUP000002593 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1515Removed in mature form; by autocatalysisUniRule annotationPRO_0000397316Add
BLAST
Chaini16 – 212197Proteasome subunit beta 2PRO_0000397317Add
BLAST

Keywords - PTMi

Autocatalytic cleavage, Zymogen

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. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN.UniRule annotation

Protein-protein interaction databases

STRINGi415426.Hbut_1567.

Structurei

3D structure databases

ProteinModelPortaliA2BN27.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091083.
KOiK03433.
OMAiHEPVIDD.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_02113_A. Proteasome_B_A.
InterProiIPR029055. Ntn_hydrolases_N.
IPR019983. Pept_T1A_Psome_bsu_arc.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03634. arc_protsome_B. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A2BN27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLHHPGTGQL RALKGTTTVG IVFRDFVVLA ADRRATAGYF VAHKRTKKII
60 70 80 90 100
KITDYMAMTT AGLVADAQML AEWLANHTHY YEIVNKRRMS IHAAAQYLSI
110 120 130 140 150
ILHSAKFYPY IVQLLLGGYD TQPRLYNIDW FGSVTEEKYV ATGSGSPTAI
160 170 180 190 200
GVIEDQYSPN LSMEEAVELA KRAVASSIRR DTFTGNGVDV VVIGKDFYRE
210
YSFELKDILK TK
Length:212
Mass (Da):23,761
Last modified:February 20, 2007 - v1
Checksum:iE276C1BD3E11D0B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000493 Genomic DNA. Translation: ABM81388.1.
RefSeqiWP_011822706.1. NC_008818.1.
YP_001013733.1. NC_008818.1.

Genome annotation databases

EnsemblBacteriaiABM81388; ABM81388; Hbut_1567.
GeneIDi4782914.
KEGGihbu:Hbut_1567.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000493 Genomic DNA. Translation: ABM81388.1.
RefSeqiWP_011822706.1. NC_008818.1.
YP_001013733.1. NC_008818.1.

3D structure databases

ProteinModelPortaliA2BN27.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi415426.Hbut_1567.

Protein family/group databases

MEROPSiT01.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM81388; ABM81388; Hbut_1567.
GeneIDi4782914.
KEGGihbu:Hbut_1567.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091083.
KOiK03433.
OMAiHEPVIDD.

Enzyme and pathway databases

BioCyciHBUT415426:GC56-1567-MONOMER.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_02113_A. Proteasome_B_A.
InterProiIPR029055. Ntn_hydrolases_N.
IPR019983. Pept_T1A_Psome_bsu_arc.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03634. arc_protsome_B. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
    Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
    Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 5456 / JCM 9403.

Entry informationi

Entry nameiPSB2_HYPBU
AccessioniPrimary (citable) accession number: A2BN27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: February 20, 2007
Last modified: July 22, 2015
This is version 61 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

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.