UniProtKB - P9WHN5 (PUP_MYCTU)
Protein
Prokaryotic ubiquitin-like protein Pup
Gene
pup
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation. Among the identified substrates are the FabD, PanB and Mpa proteins.3 Publications
Miscellaneous
The glutamate must be located at the C-terminal position to be coupled to the lysine substrate.
Fusion of Pup to a nonproteasome substrate targets it for proteasomal degradation in an Mpa- and proteasome-dependent manner.
: proteasomal Pup-dependent pathway Pathwayi
This protein is involved in the pathway proteasomal Pup-dependent pathway, which is part of Protein degradation.View all proteins of this organism that are known to be involved in the pathway proteasomal Pup-dependent pathway and in Protein degradation.
GO - Molecular functioni
- proteasome binding Source: UniProtKB
- protein tag Source: UniProtKB
GO - Biological processi
- modification-dependent protein catabolic process Source: UniProtKB
- proteasomal protein catabolic process Source: UniProtKB
- protein pupylation Source: UniProtKB
Keywordsi
Biological process | Ubl conjugation pathway |
Enzyme and pathway databases
BioCyci | MetaCyc:G185E-6317-MONOMER MTBH37RV:G185E-6317-MONOMER |
UniPathwayi | UPA00997 |
Names & Taxonomyi
Protein namesi | Recommended name: Prokaryotic ubiquitin-like protein PupAlternative name(s): Bacterial ubiquitin-like modifier |
Gene namesi | Name:pup Ordered Locus Names:Rv2111c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv2111c |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000383476 | 1 – 64 | Prokaryotic ubiquitin-like protein PupAdd BLAST | 64 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 64 | Deamidated glutamine; alternate1 Publication | 1 | |
Cross-linki | 64 | Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in acceptor proteins); alternate |
Post-translational modificationi
Is modified by deamidation of its C-terminal glutamine to glutamate by the deamidase Dop, a prerequisite to the subsequent pupylation process.1 Publication
Keywords - PTMi
Isopeptide bondProteomic databases
PaxDbi | P9WHN5 |
Interactioni
Subunit structurei
Strongly interacts with the proteasome-associated ATPase ARC (Mpa) through a hydrophobic interface; the interacting region of Pup lies in its C-terminal half. There is one Pup binding site per Mpa hexamer ring; the K(D) measured is about 3.8 µM.
5 PublicationsBinary interactionsi
With | Entry | #Exp. | IntAct | Notes |
---|---|---|---|---|
P9WQN5 | 6 | EBI-7241023,EBI-7241067 |
Protein-protein interaction databases
IntActi | P9WHN5, 1 interactor |
MINTi | P9WHN5 |
STRINGi | 83332.Rv2111c |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WHN5 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 21 – 58 | Mpa/ARC ATPase bindingAdd BLAST | 38 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 23 – 52 | Sequence analysisAdd BLAST | 30 |
Domaini
The N-terminal unstructured half of Pup provides a signal required to initiate unfolding and degradation by the proteasome but is not needed for pupylation, while the C-terminal helical half of Pup interacts with Mpa to target proteins to the proteasome.5 Publications
Sequence similaritiesi
Belongs to the prokaryotic ubiquitin-like protein family.Curated
Keywords - Domaini
Coiled coilPhylogenomic databases
KOi | K13570 |
OMAi | AGQERME |
Family and domain databases
DisProti | DP00877 |
HAMAPi | MF_02106 Pup, 1 hit |
InterProi | View protein in InterPro IPR008515 Ubiquitin-like_Pup |
Pfami | View protein in Pfam PF05639 Pup, 1 hit |
TIGRFAMsi | TIGR03687 pupylate_cterm, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WHN5-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAQEQTKRGG GGGDDDDIAG STAAGQERRE KLTEETDDLL DEIDDVLEEN
60
AEDFVRAYVQ KGGQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | EU914921 Genomic DNA Translation: ACI25441.1 AL123456 Genomic DNA Translation: CCP44886.1 |
PIRi | B70512 |
RefSeqi | NP_216627.1, NC_000962.3 WP_003411026.1, NZ_NVQJ01000058.1 |
Genome annotation databases
EnsemblBacteriai | CCP44886; CCP44886; Rv2111c |
GeneIDi | 888788 |
KEGGi | mtu:Rv2111c mtv:RVBD_2111c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | EU914921 Genomic DNA Translation: ACI25441.1 AL123456 Genomic DNA Translation: CCP44886.1 |
PIRi | B70512 |
RefSeqi | NP_216627.1, NC_000962.3 WP_003411026.1, NZ_NVQJ01000058.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3M91 | X-ray | 1.80 | B/D | 21-63 | [»] | |
3M9D | X-ray | 4.50 | G/H/I/P/Q/R | 1-64 | [»] | |
SMRi | P9WHN5 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P9WHN5, 1 interactor |
MINTi | P9WHN5 |
STRINGi | 83332.Rv2111c |
Proteomic databases
PaxDbi | P9WHN5 |
Genome annotation databases
EnsemblBacteriai | CCP44886; CCP44886; Rv2111c |
GeneIDi | 888788 |
KEGGi | mtu:Rv2111c mtv:RVBD_2111c |
Organism-specific databases
TubercuListi | Rv2111c |
Phylogenomic databases
KOi | K13570 |
OMAi | AGQERME |
Enzyme and pathway databases
UniPathwayi | UPA00997 |
BioCyci | MetaCyc:G185E-6317-MONOMER MTBH37RV:G185E-6317-MONOMER |
Family and domain databases
DisProti | DP00877 |
HAMAPi | MF_02106 Pup, 1 hit |
InterProi | View protein in InterPro IPR008515 Ubiquitin-like_Pup |
Pfami | View protein in Pfam PF05639 Pup, 1 hit |
TIGRFAMsi | TIGR03687 pupylate_cterm, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PUP_MYCTU | |
Accessioni | P9WHN5Primary (citable) accession number: P9WHN5 Secondary accession number(s): B6DAC1 Q7D7I1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | September 18, 2019 | |
This is version 31 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references