UniProtKB - P9WNU9 (DOP_MYCTU)
Protein
Pup deamidase/depupylase
Gene
dop
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins.3 Publications
Catalytic activityi
- [prokaryotic ubiquitin-like protein]-C-terminal-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-C-terminal-L-glutamate + NH4+2 PublicationsEC:3.5.1.1192 Publications
Cofactori
ATP2 PublicationsNote: ATP is required for the deamidation and depupylation reactions but is not hydrolyzed during the reactions.2 Publications
: 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.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 8 | Magnesium 1By similarity | 1 | |
Metal bindingi | 8 | Magnesium 2By similarity | 1 | |
Metal bindingi | 93 | Magnesium 1By similarity | 1 | |
Active sitei | 95 | Proton acceptorBy similarity | 1 | |
Metal bindingi | 100 | Magnesium 1By similarity | 1 | |
Metal bindingi | 156 | Magnesium 2By similarity | 1 | |
Binding sitei | 158 | ATPBy similarity | 1 | |
Binding sitei | 240 | ATPBy similarity | 1 | |
Metal bindingi | 242 | Magnesium 2By similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 6 – 10 | ATPBy similarity | 5 | |
Nucleotide bindingi | 102 – 103 | ATPBy similarity | 2 |
GO - Molecular functioni
- ATP binding Source: UniProtKB
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
- peptidase activity Source: MTBBASE
GO - Biological processi
- modification-dependent protein catabolic process Source: MTBBASE
- pathogenesis Source: UniProtKB-KW
- proteasomal protein catabolic process Source: MTBBASE
- protein pupylation Source: UniProtKB
Keywordsi
Molecular function | Hydrolase |
Biological process | Virulence |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | MetaCyc:G185E-6318-MONOMER MTBH37RV:G185E-6318-MONOMER |
UniPathwayi | UPA00997 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:dop Synonyms:pafD Ordered Locus Names:Rv2112c |
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 | Rv2112c |
Pathology & Biotechi
Disruption phenotypei
Disruption of dop abolishes pupylation. Cells lacking this gene also become hypersensitive to reactive nitrogen intermediates (RNI) and are severely attenuated for survival and growth in mice. They also cannot depupylate proteasome substrates.2 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 8 | E → A: Abolishes pupylation. 1 Publication | 1 | |
Mutagenesisi | 10 | E → A: Abolishes pupylation and depupylase activity. 2 Publications | 1 | |
Mutagenesisi | 95 | D → N: Abolishes pupylation. 1 Publication | 1 | |
Mutagenesisi | 96 | H → V: Abolishes pupylation. 1 Publication | 1 | |
Mutagenesisi | 100 | E → A: Abolishes pupylation. 1 Publication | 1 | |
Mutagenesisi | 206 | R → A: Abolishes pupylation. 1 Publication | 1 | |
Mutagenesisi | 222 | R → A: Abolishes pupylation. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000383480 | 1 – 505 | Pup deamidase/depupylaseAdd BLAST | 505 |
Proteomic databases
PaxDbi | P9WNU9 |
Interactioni
Subunit structurei
Interacts with the prokaryotic ubiquitin-like protein Pup.
2 PublicationsProtein-protein interaction databases
STRINGi | 83332.Rv2112c |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | ENOG4105E5F Bacteria ENOG410XQPS LUCA |
KOi | K20814 |
OMAi | YFRGRCL |
Family and domain databases
InterProi | View protein in InterPro IPR022366 Pup_deamidase IPR004347 Pup_ligase/deamidase |
PANTHERi | PTHR42307 PTHR42307, 1 hit |
Pfami | View protein in Pfam PF03136 Pup_ligase, 1 hit |
PIRSFi | PIRSF018077 UCP018077, 1 hit |
TIGRFAMsi | TIGR03688 pupylate_PafA2, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WNU9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MQRIIGTEVE YGISSPSDPT ANPILTSTQA VLAYAAAAGI QRAKRTRWDY
60 70 80 90 100
EVESPLRDAR GFDLSRSAGP PPVVDADEVG AANMILTNGA RLYVDHAHPE
110 120 130 140 150
YSAPECTDPL DAVIWDKAGE RVMEAAARHV ASVPGAAKLQ LYKNNVDGKG
160 170 180 190 200
ASYGSHENYL MSRQTPFSAI ITGLTPFLVS RQVVTGSGRV GIGPSGDEPG
210 220 230 240 250
FQLSQRSDYI EVEVGLETTL KRGIINTRDE PHADADRYRR LHVIIGDANL
260 270 280 290 300
AETSTYLKLG TTALVLDLIE EGPAHAIDLT DLALARPVHA VHAISRDPSL
310 320 330 340 350
RATVALADGR ELTGLALQRI YLDRVAKLVD SRDPDPRAAD IVETWAHVLD
360 370 380 390 400
QLERDPMDCA ELLDWPAKLR LLDGFRQREN LSWSAPRLHL VDLQYSDVRL
410 420 430 440 450
DKGLYNRLVA RGSMKRLVTE HQVLSAVENP PTDTRAYFRG ECLRRFGADI
460 470 480 490 500
AAASWDSVIF DLGGDSLVRI PTLEPLRGSK AHVGALLDSV DSAVELVEQL
TAEPR
Sequence cautioni
The sequence CCP44887 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44887.1 Different initiation. |
PIRi | C70512 |
RefSeqi | NP_216628.1, NC_000962.3 |
Genome annotation databases
EnsemblBacteriai | CCP44887; CCP44887; Rv2112c |
GeneIDi | 888290 |
KEGGi | mtu:Rv2112c |
PATRICi | fig|83332.12.peg.2359 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44887.1 Different initiation. |
PIRi | C70512 |
RefSeqi | NP_216628.1, NC_000962.3 |
3D structure databases
SMRi | P9WNU9 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv2112c |
Proteomic databases
PaxDbi | P9WNU9 |
Genome annotation databases
EnsemblBacteriai | CCP44887; CCP44887; Rv2112c |
GeneIDi | 888290 |
KEGGi | mtu:Rv2112c |
PATRICi | fig|83332.12.peg.2359 |
Organism-specific databases
TubercuListi | Rv2112c |
Phylogenomic databases
eggNOGi | ENOG4105E5F Bacteria ENOG410XQPS LUCA |
KOi | K20814 |
OMAi | YFRGRCL |
Enzyme and pathway databases
UniPathwayi | UPA00997 |
BioCyci | MetaCyc:G185E-6318-MONOMER MTBH37RV:G185E-6318-MONOMER |
Family and domain databases
InterProi | View protein in InterPro IPR022366 Pup_deamidase IPR004347 Pup_ligase/deamidase |
PANTHERi | PTHR42307 PTHR42307, 1 hit |
Pfami | View protein in Pfam PF03136 Pup_ligase, 1 hit |
PIRSFi | PIRSF018077 UCP018077, 1 hit |
TIGRFAMsi | TIGR03688 pupylate_PafA2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DOP_MYCTU | |
Accessioni | P9WNU9Primary (citable) accession number: P9WNU9 Secondary accession number(s): L0TBE2, O33247, Q8VJQ0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | October 16, 2019 | |
This is version 35 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
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