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A0QZ47 (PSB_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 beta

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit
Proteasome core protein PrcB
Gene names
Name:prcB
Ordered Locus Names:MSMEG_3895, MSMEI_3805
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length303 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 M.smegmatis proteasome is able to cleave oligopeptides after hydrophobic residues, thus displaying chymotrypsin-like activity. Among the identified substrates of the M.smegmatis proteasome are the pupylated SodA and Ino1 proteins. Ref.1 Ref.5

Catalytic activity

Cleavage of peptide bonds with very broad specificity. Ref.1 Ref.5

Enzyme regulation

The formation of the proteasomal ATPase ARC-20S proteasome complex, likely via the docking of the C-termini of ARC into the intersubunit pockets in the alpha-rings, may trigger 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. Peptidolytic activity is inhibited by N-acetyl-Leu-Leu-norleucinal (Ac-LLnL) in vitro. Ref.1

Pathway

Protein degradation; proteasomal Pup-dependent pathway. HAMAP-Rule MF_02113

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. 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 by the proteasome-associated ATPase, ARC By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02113.

Disruption phenotype

Cells lacking this gene are viable and grow at the wild-type rate, but show a large reduction in the rate of degradation of the pupylated substrates. Ref.1 Ref.5

Sequence similarities

Belongs to the peptidase T1B family.

Sequence caution

The sequence ABK70234.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 6262Removed in mature form; by autocatalysis By similarity
PRO_0000383487
Chain63 – 303241Proteasome subunit beta HAMAP-Rule MF_02113
PRO_0000383488

Sites

Active site631Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QZ47 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: F464A036F8CD459C

FASTA30332,131
        10         20         30         40         50         60 
MTWRDNQSFP QPTLNTTGIP SVPVDLSSFS ELLSRQAPEL LPVNRVAYGT TPVGPTDAVP 

        70         80         90        100        110        120 
HGTTIVALKY PGGVLIAGDR RSTQGNMIAG RDVQKVYITD DYTATGIAGT AAIAVEFARL 

       130        140        150        160        170        180 
YAVELEHYEK LEGVPLTFRG KVNRLAIMVR GNLGAALQGF VALPLLVGYD LDDPHPEGAG 

       190        200        210        220        230        240 
RIVSFDAAGG WNIEEEGYQS VGSGSIFAKS SMKKLYSQVS DADSALKVAV EALYDAADDD 

       250        260        270        280        290        300 
SATGGPDLVR GIYPTAVTIG AEGAEEVPET RIAELAREVI ESRSRTDTFG PDARRGIDAR 


GDS 

« Hide

References

« Hide 'large scale' references
[1]"Inactivation of the 20S proteasome in Mycobacterium smegmatis."
Knipfer N., Shrader T.E.
Mol. Microbiol. 25:375-383(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, DISRUPTION PHENOTYPE.
[2]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[4]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[5]"Proteasomal protein degradation in mycobacteria is dependent upon a prokaryotic ubiquitin-like protein."
Burns K.E., Liu W.-T., Boshoff H.I.M., Dorrestein P.C., Barry C.E. III
J. Biol. Chem. 284:3069-3075(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, PROTEIN SUBSTRATES, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF009645 Genomic DNA. Translation: AAC45614.1.
CP000480 Genomic DNA. Translation: ABK70234.1. Different initiation.
CP001663 Genomic DNA. Translation: AFP40263.1.
RefSeqYP_006568558.1. NC_018289.1.
YP_888185.1. NC_008596.1.

3D structure databases

ProteinModelPortalA0QZ47.
SMRA0QZ47. Positions 25-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246196.MSMEG_3895.

Protein family/group databases

MEROPST01.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK70234; ABK70234; MSMEG_3895.
AFP40263; AFP40263; MSMEI_3805.
GeneID4534165.
KEGGmsg:MSMEI_3805.
msm:MSMEG_3895.
PATRIC18080185. VBIMycSme59918_3835.

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000245308.
KOK03433.
OrthoDBEOG6XM79W.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-3894-MONOMER.
UniPathwayUPA00997.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
HAMAPMF_02113_B. Proteasome_B_B.
InterProIPR029055. Ntn_hydrolases_N.
IPR022483. Pept_T1A_Psome_suB_actinobac.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR03690. 20S_bact_beta. 1 hit.
PROSITEPS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSB_MYCS2
AccessionPrimary (citable) accession number: A0QZ47
Secondary accession number(s): I7FNI5, O30518
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 22, 2009
Last modified: July 9, 2014
This is version 62 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways