MULTISPECIES: ubiquitin-like protein Pup [Mycobacterium]
Protein Classification
ubiquitin-like protein Pup( domain architecture ID 10528993)
ubiquitin-like protein Pup is a protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Pup | pfam05639 | Pup-like protein; This family consists of several short bacterial proteins formely known as ... |
3-64 | 2.17e-16 | ||
Pup-like protein; This family consists of several short bacterial proteins formely known as (DUF797). It was recently shown that Mycobacterium tuberculosis contains a small protein, Pup (Rv2111c), that is covalently conjugated to the e-NH2 groups of lysines on several target proteins (pupylation) such as the malonyl CoA acyl carrier protein (FabD). Pupylation of FabD was shown to result in its recruitment to the mycobacterial proteasome and subsequent degradation analogous to eukaryotic ubiquitin-conjugated proteins. Searches recovered Pup orthologs in all major actinobacteria lineages including the basal bifidobacteria and also sporadically in certain other bacterial lineages. The Pup proteins were all between 50-90 residues in length and a multiple alignment shows that they all contain a conserved motif with a G [EQ] signature at the C-terminus. Thus, all of them are suitable for conjugation via the terminal glutamate or the deamidated glutamine (as shown in the case of the Mycobacterium). The conserved globular core of Pup is predicted to form a bihelical unit with the extreme C-terminal 6-7 residues forming a tail in the extended conformation. Thus, Pup is structurally unrelated to the ubiquitin fold and has convergently evolved the function of protein modifier. : Pssm-ID: 428558 Cd Length: 64 Bit Score: 65.46 E-value: 2.17e-16
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| Name | Accession | Description | Interval | E-value | ||
| Pup | pfam05639 | Pup-like protein; This family consists of several short bacterial proteins formely known as ... |
3-64 | 2.17e-16 | ||
Pup-like protein; This family consists of several short bacterial proteins formely known as (DUF797). It was recently shown that Mycobacterium tuberculosis contains a small protein, Pup (Rv2111c), that is covalently conjugated to the e-NH2 groups of lysines on several target proteins (pupylation) such as the malonyl CoA acyl carrier protein (FabD). Pupylation of FabD was shown to result in its recruitment to the mycobacterial proteasome and subsequent degradation analogous to eukaryotic ubiquitin-conjugated proteins. Searches recovered Pup orthologs in all major actinobacteria lineages including the basal bifidobacteria and also sporadically in certain other bacterial lineages. The Pup proteins were all between 50-90 residues in length and a multiple alignment shows that they all contain a conserved motif with a G [EQ] signature at the C-terminus. Thus, all of them are suitable for conjugation via the terminal glutamate or the deamidated glutamine (as shown in the case of the Mycobacterium). The conserved globular core of Pup is predicted to form a bihelical unit with the extreme C-terminal 6-7 residues forming a tail in the extended conformation. Thus, Pup is structurally unrelated to the ubiquitin fold and has convergently evolved the function of protein modifier. Pssm-ID: 428558 Cd Length: 64 Bit Score: 65.46 E-value: 2.17e-16
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| pupylate_cterm | TIGR03687 | ubiquitin-like protein Pup; Members of this protein family are Pup, a small protein whose ... |
32-64 | 1.54e-10 | ||
ubiquitin-like protein Pup; Members of this protein family are Pup, a small protein whose ligation to target proteins steers them toward degradation. This protein family occurs in a number of bacteria, especially Actinobacteria such as Mycobacterium tuberculosis, that possess an archeal-type proteasome. All members of this protein family known during model construction end with the C-terminal motif [FY][VI]QKGG[QE]. Ligation is thought to occur between the C-terminal COOH of Pup and an epsilon-amino group of a Lys on the target protein. The N-terminal half of this protein is poorly conserved and not represented in the seed alignment. [Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 200311 Cd Length: 33 Bit Score: 50.13 E-value: 1.54e-10
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| Name | Accession | Description | Interval | E-value | ||
| Pup | pfam05639 | Pup-like protein; This family consists of several short bacterial proteins formely known as ... |
3-64 | 2.17e-16 | ||
Pup-like protein; This family consists of several short bacterial proteins formely known as (DUF797). It was recently shown that Mycobacterium tuberculosis contains a small protein, Pup (Rv2111c), that is covalently conjugated to the e-NH2 groups of lysines on several target proteins (pupylation) such as the malonyl CoA acyl carrier protein (FabD). Pupylation of FabD was shown to result in its recruitment to the mycobacterial proteasome and subsequent degradation analogous to eukaryotic ubiquitin-conjugated proteins. Searches recovered Pup orthologs in all major actinobacteria lineages including the basal bifidobacteria and also sporadically in certain other bacterial lineages. The Pup proteins were all between 50-90 residues in length and a multiple alignment shows that they all contain a conserved motif with a G [EQ] signature at the C-terminus. Thus, all of them are suitable for conjugation via the terminal glutamate or the deamidated glutamine (as shown in the case of the Mycobacterium). The conserved globular core of Pup is predicted to form a bihelical unit with the extreme C-terminal 6-7 residues forming a tail in the extended conformation. Thus, Pup is structurally unrelated to the ubiquitin fold and has convergently evolved the function of protein modifier. Pssm-ID: 428558 Cd Length: 64 Bit Score: 65.46 E-value: 2.17e-16
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| pupylate_cterm | TIGR03687 | ubiquitin-like protein Pup; Members of this protein family are Pup, a small protein whose ... |
32-64 | 1.54e-10 | ||
ubiquitin-like protein Pup; Members of this protein family are Pup, a small protein whose ligation to target proteins steers them toward degradation. This protein family occurs in a number of bacteria, especially Actinobacteria such as Mycobacterium tuberculosis, that possess an archeal-type proteasome. All members of this protein family known during model construction end with the C-terminal motif [FY][VI]QKGG[QE]. Ligation is thought to occur between the C-terminal COOH of Pup and an epsilon-amino group of a Lys on the target protein. The N-terminal half of this protein is poorly conserved and not represented in the seed alignment. [Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 200311 Cd Length: 33 Bit Score: 50.13 E-value: 1.54e-10
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