DOP_MYCTO
ID DOP_MYCTO Reviewed; 505 AA.
AC P9WNU8; L0TBE2; O33247; Q8VJQ0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Pup deamidase/depupylase;
DE EC=3.4.-.-;
DE EC=3.5.1.119 {ECO:0000250|UniProtKB:P9WNU9};
DE AltName: Full=Deamidase of protein Pup;
GN Name=dop; Synonyms=pafD; OrderedLocusNames=MT2172;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Specifically catalyzes the deamidation of the C-terminal
CC glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate,
CC thereby rendering Pup competent for conjugation. Also displays
CC depupylase (DPUP) activity, removing conjugated Pup from target
CC proteins; is thus involved in the recycling of Pup and may function
CC similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote
CC proteasomal degradation of certain proteins.
CC {ECO:0000250|UniProtKB:P9WNU9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[prokaryotic ubiquitin-like protein]-C-terminal-L-glutamine +
CC H2O = [prokaryotic ubiquitin-like protein]-C-terminal-L-glutamate +
CC NH4(+); Xref=Rhea:RHEA:47952, Rhea:RHEA-COMP:11959, Rhea:RHEA-
CC COMP:11960, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:78525,
CC ChEBI:CHEBI:88115; EC=3.5.1.119;
CC Evidence={ECO:0000250|UniProtKB:P9WNU9};
CC -!- COFACTOR:
CC Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000250};
CC Note=ATP is required for the deamidation and depupylation reactions but
CC is not hydrolyzed during the reactions. {ECO:0000250};
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC -!- SUBUNIT: Interacts with the prokaryotic ubiquitin-like protein Pup.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Pup ligase/Pup deamidase family. Pup
CC deamidase subfamily. {ECO:0000305}.
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DR EMBL; AE000516; AAK46455.1; -; Genomic_DNA.
DR PIR; C70512; C70512.
DR RefSeq; WP_003411029.1; NC_002755.2.
DR AlphaFoldDB; P9WNU8; -.
DR SMR; P9WNU8; -.
DR EnsemblBacteria; AAK46455; AAK46455; MT2172.
DR KEGG; mtc:MT2172; -.
DR HOGENOM; CLU_040524_1_0_11; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR InterPro; IPR022366; Pup_deamidase.
DR InterPro; IPR004347; Pup_ligase/deamidase.
DR PANTHER; PTHR42307; PTHR42307; 1.
DR Pfam; PF03136; Pup_ligase; 1.
DR PIRSF; PIRSF018077; UCP018077; 1.
DR TIGRFAMs; TIGR03688; pupylate_PafA2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW Virulence.
FT CHAIN 1..505
FT /note="Pup deamidase/depupylase"
FT /id="PRO_0000427064"
FT ACT_SITE 95
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 6..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 102..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 505 AA; 55179 MW; 963CF8592FC182EB CRC64;
MQRIIGTEVE YGISSPSDPT ANPILTSTQA VLAYAAAAGI QRAKRTRWDY EVESPLRDAR
GFDLSRSAGP PPVVDADEVG AANMILTNGA RLYVDHAHPE YSAPECTDPL DAVIWDKAGE
RVMEAAARHV ASVPGAAKLQ LYKNNVDGKG ASYGSHENYL MSRQTPFSAI ITGLTPFLVS
RQVVTGSGRV GIGPSGDEPG FQLSQRSDYI EVEVGLETTL KRGIINTRDE PHADADRYRR
LHVIIGDANL AETSTYLKLG TTALVLDLIE EGPAHAIDLT DLALARPVHA VHAISRDPSL
RATVALADGR ELTGLALQRI YLDRVAKLVD SRDPDPRAAD IVETWAHVLD QLERDPMDCA
ELLDWPAKLR LLDGFRQREN LSWSAPRLHL VDLQYSDVRL DKGLYNRLVA RGSMKRLVTE
HQVLSAVENP PTDTRAYFRG ECLRRFGADI AAASWDSVIF DLGGDSLVRI PTLEPLRGSK
AHVGALLDSV DSAVELVEQL TAEPR
