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A9A4A1 (PSB1_NITMS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 1

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit 1
Proteasome core protein PsmB 1
Gene names
Name:psmB1
Ordered Locus Names:Nmar_0694
OrganismNitrosopumilus maritimus (strain SCM1) [Reference proteome] [HAMAP]
Taxonomic identifier436308 [NCBI]
Taxonomic lineageArchaeaThaumarchaeotaNitrosopumilalesNitrosopumilaceaeNitrosopumilus

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation By similarity. HAMAP-Rule MF_02113

Catalytic activity

Cleavage of peptide bonds with very broad specificity. HAMAP-Rule MF_02113

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. 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 at one or both ends by the proteasome regulatory ATPase, PAN By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02113.

Sequence similarities

Belongs to the peptidase T1B family.

Ontologies

Keywords
   Cellular componentCytoplasm
Proteasome
   Molecular functionHydrolase
Protease
Threonine protease
   PTMAutocatalytic cleavage
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteasomal protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteasome core complex, beta-subunit complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionthreonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 88Removed in mature form; by autocatalysis Potential
PRO_0000397388
Chain9 – 198190Proteasome subunit beta 1 HAMAP-Rule MF_02113
PRO_0000397389

Sites

Active site91Nucleophile Potential

Sequences

Sequence LengthMass (Da)Tools
A9A4A1 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 26D6CEB86D6B4D32

FASTA19821,330
        10         20         30         40         50         60 
MSMYMPGATA VGITFDGGVV FASEKRIAFG NFLVSKTTKK TFPITPKVGA TCAGLVADMQ 

        70         80         90        100        110        120 
ILSLQIAALA KIRKMELKRD VPPNTVAKMM SNMMYERRYF PLLTQVIVGG VVDKPIMYTL 

       130        140        150        160        170        180 
DPLGSVLPDE YAAVGTGAEM ALGVLDPQFK PNMTKDEAID LAKRAVRAAS LRDSASGDGV 

       190 
DVLVITKDGT EEFTEEIK 

« Hide

References

[1]"Complete sequence of Nitrosopumilus maritimus SCM1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Stahl D., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SCM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000866 Genomic DNA. Translation: ABX12590.1.
RefSeqYP_001582028.1. NC_010085.1.

3D structure databases

ProteinModelPortalA9A4A1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436308.Nmar_0694.

Protein family/group databases

MEROPST01.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX12590; ABX12590; Nmar_0694.
GeneID5774004.
KEGGnmr:Nmar_0694.

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091083.
KOK03433.
OMAYSYKLAP.

Enzyme and pathway databases

BioCycNMAR436308:GI3J-719-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.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSB1_NITMS
AccessionPrimary (citable) accession number: A9A4A1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: January 15, 2008
Last modified: June 11, 2014
This is version 39 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