A1RX71 (PSB2_THEPD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome subunit beta 2
EC=3.4.25.1

Alternative name(s):
20S proteasome beta subunit 2
Proteasome core protein PsmB 2

Gene names

Name:	psmB2
Ordered Locus Names:	Tpen_0392

Organism

Thermofilum pendens (strain Hrk 5) [Reference proteome] [HAMAP]

Taxonomic identifier

368408 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermofilaceae › Thermofilum › Thermofilum pendens

Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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.
Sequence similarities	Belongs to the peptidase T1B family.

Ontologies

Keywords
Cellular component	Cytoplasm Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Autocatalytic cleavage Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteasomal protein catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex, beta-subunit complex Inferred from electronic annotation. Source: HAMAP
Molecular_function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 6	6	Removed in mature form; by autocatalysis Potential		PRO_0000397478
	Chain	7 – 204	198	Proteasome subunit beta 2 HAMAP-Rule MF_02113		PRO_0000397479
Sites
	Active site	7	1	Nucleophile Potential

Sequences

	Sequence		Length	Mass (Da)
	A1RX71 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: AF45C4D4B1508252	FASTA	204	22,161
	10 20 30 40 50 60 MEVLPGTTVG IRVSDGVVLA AEKRVSYGLY LMSKSGKKVY RILDKMGMAS AGLMADMQTL 70 80 90 100 110 120 ARIVEAEMRL YELDSNISPK VWTVAKLLSY ILYERRLFPY YAEIVVGGLD EEGSHLYSLD 130 140 150 160 170 180 PIGAIIEDDY VALGSGTQLA ISIVESNYKK DMSLDEALSL ALKSVYAAMK RDAASGDGVD 190 200 VLVIGKSGTL EKTYPLSELQ SVAV

References

[1]

"Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction." Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E., Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M., Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B. , Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N. J. Bacteriol. 190:2957-2965(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hrk 5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000505 Genomic DNA. Translation: ABL77801.1.
RefSeq	YP_919804.1. NC_008698.1.
3D structure databases
ProteinModelPortal	A1RX71.
ModBase	Search...
Protein-protein interaction databases
STRING	368408.Tpen_0392.
Protein family/group databases
MEROPS	T01.002.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABL77801; ABL77801; Tpen_0392.
GeneID	4600527.
KEGG	tpe:Tpen_0392.
Phylogenomic databases
eggNOG	COG0638.
HOGENOM	HOG000091083.
KO	K03433.
OMA	KMSCPAM.
Family and domain databases
HAMAP	MF_02113_A. Proteasome_B_A.
InterPro	IPR019983. Pept_T1A_Psome_bsu_arc. IPR000243. Pept_T1A_subB. IPR016050. Proteasome_bsu_CS. IPR001353. Proteasome_sua/b. IPR023333. Proteasome_suB-type. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
PRINTS	PR00141. PROTEASOME.
TIGRFAMs	TIGR03634. arc_protsome_B. 1 hit.
PROSITE	PS00854. PROTEASOME_B_1. 1 hit. PS51476. PROTEASOME_B_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PSB2_THEPD

Accession

Primary (citable) accession number: A1RX71

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 10, 2010
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program