Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Belongs to the Bpa family.

Probable AAA-family ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Belongs to the Bpa family.

Conserved hypothetical protein; Highly similar to many proteins of undefined function including: Rhodococcus sp. TR:Q53081 (EMBL:U26422) (499 aa); Fasta score E(): 0, 83.5% identity in 502 aa overlap and Mycobacterium tuberculosis RV2112C TR:O33247 (EMBL:Z97559) (554 aa); Fasta score E(): 0, 95.4% identity in 504 aa overlap.

Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Belongs to the Bpa family.

Conserved hypothetical protein; Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation.

Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Belongs to the Bpa family.

Possible DNA-binding protein; Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side- chain amino group of a substrate lysine.

Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Belongs to the Bpa family.

Proteasome [alpha]-type subunit 1; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. Belongs to the peptidase T1A family.

Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Belongs to the Bpa family.

Proteasome [beta]-type subunit 2; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. Belongs to the peptidase T1B family.

Conserved hypothetical protein; Similar to several proteins of unkown function including: Mycobacterium tuberculosis RV2125 TR:O33260 (EMBL:Z97559) (292 aa); Fasta score E(): 0, 85.0% identity in 274 aa overlap and Streptomyces coelicolor TR:Q9S2K6 (EMBL:AL109732) (312 aa); Fasta score E(): 1.6e-07, 23.4% identity in 278 aa overlap.

Proteasome [beta]-type subunit 2; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. Belongs to the peptidase T1B family.

Probable AAA-family ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Belongs to the Bpa family.

Probable AAA-family ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

Conserved hypothetical protein; Highly similar to many proteins of undefined function including: Rhodococcus sp. TR:Q53081 (EMBL:U26422) (499 aa); Fasta score E(): 0, 83.5% identity in 502 aa overlap and Mycobacterium tuberculosis RV2112C TR:O33247 (EMBL:Z97559) (554 aa); Fasta score E(): 0, 95.4% identity in 504 aa overlap.

Probable AAA-family ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

Conserved hypothetical protein; Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation.

Probable AAA-family ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

Possible DNA-binding protein; Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side- chain amino group of a substrate lysine.

Probable AAA-family ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

Proteasome [alpha]-type subunit 1; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. Belongs to the peptidase T1A family.

Probable AAA-family ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

Proteasome [beta]-type subunit 2; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. Belongs to the peptidase T1B family.

Conserved hypothetical protein; Highly similar to many proteins of undefined function including: Rhodococcus sp. TR:Q53081 (EMBL:U26422) (499 aa); Fasta score E(): 0, 83.5% identity in 502 aa overlap and Mycobacterium tuberculosis RV2112C TR:O33247 (EMBL:Z97559) (554 aa); Fasta score E(): 0, 95.4% identity in 504 aa overlap.

Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Belongs to the Bpa family.

Conserved hypothetical protein; Highly similar to many proteins of undefined function including: Rhodococcus sp. TR:Q53081 (EMBL:U26422) (499 aa); Fasta score E(): 0, 83.5% identity in 502 aa overlap and Mycobacterium tuberculosis RV2112C TR:O33247 (EMBL:Z97559) (554 aa); Fasta score E(): 0, 95.4% identity in 504 aa overlap.

Probable AAA-family ATPase; ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.

Conserved hypothetical protein; Highly similar to many proteins of undefined function including: Rhodococcus sp. TR:Q53081 (EMBL:U26422) (499 aa); Fasta score E(): 0, 83.5% identity in 502 aa overlap and Mycobacterium tuberculosis RV2112C TR:O33247 (EMBL:Z97559) (554 aa); Fasta score E(): 0, 95.4% identity in 504 aa overlap.

Conserved hypothetical protein; Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation.

Conserved hypothetical protein; Highly similar to many proteins of undefined function including: Rhodococcus sp. TR:Q53081 (EMBL:U26422) (499 aa); Fasta score E(): 0, 83.5% identity in 502 aa overlap and Mycobacterium tuberculosis RV2112C TR:O33247 (EMBL:Z97559) (554 aa); Fasta score E(): 0, 95.4% identity in 504 aa overlap.

Possible DNA-binding protein; Similar to Mycobacterium tuberculosis hypothetical 79.7 kda protein TR:O53874 (EMBL:AL022004) fasta scores: E(): 0, 77.6% in 753 aa, and to Streptomyces coelicolor hypothetical 90.4 kda protein TR:CAB93395 (EMBL:AL357524) fasta scores: E(): 3.9e-27, 34.6% in 856 aa. Contains a probable helix-turn-helix motif at aa 277-298 (Score 1075, SD +2.85).

Conserved hypothetical protein; Highly similar to many proteins of undefined function including: Rhodococcus sp. TR:Q53081 (EMBL:U26422) (499 aa); Fasta score E(): 0, 83.5% identity in 502 aa overlap and Mycobacterium tuberculosis RV2112C TR:O33247 (EMBL:Z97559) (554 aa); Fasta score E(): 0, 95.4% identity in 504 aa overlap.

Proteasome [alpha]-type subunit 1; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. Belongs to the peptidase T1A family.

Conserved hypothetical protein; Highly similar to many proteins of undefined function including: Rhodococcus sp. TR:Q53081 (EMBL:U26422) (499 aa); Fasta score E(): 0, 83.5% identity in 502 aa overlap and Mycobacterium tuberculosis RV2112C TR:O33247 (EMBL:Z97559) (554 aa); Fasta score E(): 0, 95.4% identity in 504 aa overlap.

Proteasome [beta]-type subunit 2; Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. Belongs to the peptidase T1B family.

Conserved hypothetical protein; Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation.

Conserved hypothetical protein; Interacts with the core proteasome alpha-subunit (PrcA) through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif). Interaction of Bpa with the proteasome stimulates proteosomal peptidase and casein degradation activity, which suggests Bpa could play a role in the removal of non-native or damaged proteins by influencing the conformation of the proteasome complex upon interaction. Belongs to the Bpa family.