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Protein

Proteasome subunit beta 2

Gene

psmB2

Organism
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
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 sitei7 – 71NucleophileUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. proteasomal protein catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciMSED399549:GH1O-2313-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:Msed_2268
OrganismiMetallosphaera sedula (strain ATCC 51363 / DSM 5348)
Taxonomic identifieri399549 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera
ProteomesiUP000000242: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. proteasome core complex, beta-subunit complex Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 66Removed in mature form; by autocatalysisUniRule annotationPRO_0000397328
Chaini7 – 196190Proteasome subunit beta 2PRO_0000397329Add
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

STRINGi399549.Msed_2268.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091083.
KOiK03433.
OMAiGRELTIK.

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.
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.
PROSITEiPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A4YJ04-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEELPSTAVG IRLQDGVILG AVRRLSYGGY VLSKSAKKVF PISRFGIGGA
60 70 80 90 100
GLFGDLQALT RIMNANIKYY ELYNNRPIST RAAAKLLSII LYQYKYMPFI
110 120 130 140 150
SEVLFGGVDN GEPQLYVLDP LGSLLDDIYA AVGSGARVAI GVLEAEYSEK
160 170 180 190
LTLTQGRELT IKSLRASAER DVTSGDGIDI LTISKDGKIN TEFLSS
Length:196
Mass (Da):21,236
Last modified:May 29, 2007 - v1
Checksum:i8B4FD5AA1F73ABF6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000682 Genomic DNA. Translation: ABP96406.1.
RefSeqiWP_012022193.1. NC_009440.1.
YP_001192330.1. NC_009440.1.

Genome annotation databases

EnsemblBacteriaiABP96406; ABP96406; Msed_2268.
GeneIDi5104220.
KEGGimse:Msed_2268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000682 Genomic DNA. Translation: ABP96406.1.
RefSeqiWP_012022193.1. NC_009440.1.
YP_001192330.1. NC_009440.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi399549.Msed_2268.

Protein family/group databases

MEROPSiT01.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP96406; ABP96406; Msed_2268.
GeneIDi5104220.
KEGGimse:Msed_2268.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091083.
KOiK03433.
OMAiGRELTIK.

Enzyme and pathway databases

BioCyciMSED399549:GH1O-2313-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.
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.
PROSITEiPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
    Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
    Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51363 / DSM 5348.

Entry informationi

Entry nameiPSB2_METS5
AccessioniPrimary (citable) accession number: A4YJ04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: May 29, 2007
Last modified: February 4, 2015
This is version 52 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.