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Protein

Proteasome subunit beta

Gene

psmB

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
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 T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.1 Publication

Miscellaneous

The configuration of the closed gate contains an opening large enough to allow rapid entry of tetrapeptides but able to impede the entry of proteins and longer peptides.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.1 Publication

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.2 Publications

Kineticsi

  1. KM=39 µM for Suc-LLVY-Amc (at 55 degrees Celsius)1 Publication
  1. Vmax=28 nmol/min/mg enzyme with Suc-LLVY-Amc as substrate (at 55 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei9Nucleophile1 Publication1

GO - Molecular functioni

  • endopeptidase activity Source: UniProtKB
  • threonine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • proteasomal protein catabolic process Source: UniProtKB

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease

Protein family/group databases

MEROPSiT01.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta (EC:3.4.25.1)
Alternative name(s):
20S proteasome beta subunit
Proteasome core protein PsmB
Gene namesi
Name:psmB
Ordered Locus Names:Ta0612
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • proteasome core complex, beta-subunit complex Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9T → S: No effect on catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000266751 – 8Removed in mature form; by autocatalysis1 Publication8
ChainiPRO_00000266769 – 211Proteasome subunit betaAdd BLAST203

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Proteomic databases

PRIDEiP28061.

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.6 Publications

Protein-protein interaction databases

STRINGi273075.Ta0612.

Structurei

Secondary structure

1211
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 16Combined sources6
Beta strandi19 – 24Combined sources6
Beta strandi28 – 30Combined sources3
Beta strandi33 – 37Combined sources5
Beta strandi42 – 46Combined sources5
Beta strandi49 – 55Combined sources7
Helixi57 – 78Combined sources22
Helixi84 – 97Combined sources14
Turni98 – 100Combined sources3
Beta strandi105 – 121Combined sources17
Beta strandi127 – 136Combined sources10
Helixi139 – 149Combined sources11
Helixi156 – 173Combined sources18
Beta strandi174 – 176Combined sources3
Beta strandi182 – 187Combined sources6
Turni188 – 190Combined sources3
Beta strandi191 – 194Combined sources4
Helixi197 – 207Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PMAX-ray3.401/2/B/P/Q/R/S/T/U/V/W/X/Y/Z1-211[»]
1YA7X-ray2.30H/I/J/K/L/M/N1-211[»]
1YARX-ray1.90H/I/J/K/L/M/N1-211[»]
1YAUX-ray2.40H/I/J/K/L/M/N1-211[»]
3C91electron microscopy6.801/2/H/I/J/K/L/M/N/V/W/X/Y/Z9-211[»]
3C92electron microscopy6.801/2/H/I/J/K/L/M/N/V/W/X/Y/Z9-211[»]
3IPMX-ray4.00H/I/J/K/L/M/N1-211[»]
3J9Ielectron microscopy3.301/2/H/I/J/K/L/M/N/V/W/X/Y/Z9-211[»]
3JRMX-ray2.90H/I/J/K/L/M/N9-211[»]
3JSEX-ray2.90H/I/J/K/L/M/N9-211[»]
3JTLX-ray3.20H/I/J/K/L/M/N9-211[»]
5VY3electron microscopy3.101/B/D/F/H/J/L/N/P/R/T/V/X/Z9-211[»]
5VY4electron microscopy3.301/B/D/F/H/J/L/N/P/R/T/V/X/Z9-211[»]
ProteinModelPortaliP28061.
SMRiP28061.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28061.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

eggNOGiarCOG00970. Archaea.
COG0638. LUCA.
HOGENOMiHOG000091083.
KOiK03433.
OMAiDLCVIRK.
OrthoDBiPOG093Z0CM8.

Family and domain databases

CDDicd03764. proteasome_beta_archeal. 1 hit.
Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_02113_A. Proteasome_B_A. 1 hit.
InterProiView protein in InterPro
IPR029055. 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.
PANTHERiPTHR11599:SF108. PTHR11599:SF108. 1 hit.
PfamiView protein in Pfam
PF00227. Proteasome. 1 hit.
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03634. arc_protsome_B. 1 hit.
PROSITEiView protein in PROSITE
PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P28061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQTLETGTT TVGITLKDAV IMATERRVTM ENFIMHKNGK KLFQIDTYTG
60 70 80 90 100
MTIAGLVGDA QVLVRYMKAE LELYRLQRRV NMPIEAVATL LSNMLNQVKY
110 120 130 140 150
MPYMVQLLVG GIDTAPHVFS IDAAGGSVED IYASTGSGSP FVYGVLESQY
160 170 180 190 200
SEKMTVDEGV DLVIRAISAA KQRDSASGGM IDVAVITRKD GYVQLPTDQI
210
ESRIRKLGLI L
Length:211
Mass (Da):23,147
Last modified:August 1, 1992 - v1
Checksum:iF81B9360641873DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83674 Genomic DNA. Translation: AAA72102.1.
AL445064 Genomic DNA. Translation: CAC11751.1.
PIRiA42068.
RefSeqiWP_010901036.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC11751; CAC11751; CAC11751.
GeneIDi1456195.
KEGGitac:Ta0612.

Similar proteinsi

Entry informationi

Entry nameiPSB_THEAC
AccessioniPrimary (citable) accession number: P28061
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 25, 2017
This is version 131 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families