DOP_RHOER
ID DOP_RHOER Reviewed; 499 AA.
AC Q53081;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 63.
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;
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=1833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NI86/21;
RX PubMed=7583123; DOI=10.1016/s0960-9822(95)00153-9;
RA Tamura T., Nagy I., Lupas A., Lottspeich F., Cejka Z., Schoofs G.,
RA Tanaka K., de Mot R., Baumeister W.;
RT "The first characterization of a eubacterial proteasome: the 20S complex of
RT Rhodococcus.";
RL Curr. Biol. 5:766-774(1995).
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 -!- SIMILARITY: Belongs to the Pup ligase/Pup deamidase family. Pup
CC deamidase subfamily. {ECO:0000305}.
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DR EMBL; U26422; AAC45734.1; -; Genomic_DNA.
DR RefSeq; WP_019748516.1; NZ_WIDN01000105.1.
DR AlphaFoldDB; Q53081; -.
DR SMR; Q53081; -.
DR STRING; 1833.XU06_14810; -.
DR OMA; YFRGRCL; -.
DR UniPathway; UPA00997; -.
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.
FT CHAIN 1..499
FT /note="Pup deamidase/depupylase"
FT /id="PRO_0000395859"
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 499 AA; 54681 MW; 8A395271E61EB9EF CRC64;
MQRIIGVEVE YGISSPSEPS ANPILTSTQA VLAYAAAAGV PRAKRTRWDY EVESPLRDAR
GFDLGRMSGP APVIDADEIG AANMILTNGA RLYVDHAHPE YSAPEVADPL DAVIWDKAGE
RVMEAAARHA SSVPGAPRLQ LYKNNVDGKG ASYGTHENYL CSRDTPFASI VTGLTPFFAS
RQVICGSGRV GLGQSGDEAG FQLSQRSDYI EVEVGLETTL KRGIINTRDE PHADADKYRR
LHVIIGDANL AEMSTYLKVG TTALVLDLIE AGVDLTDLQL ARPVTAVHHI SHDPTLRKTV
ALADGRELTG LALQRIYLER VSKFLDREAD RDPRADDIVA KWAMVLDLLE RDPMECANIL
DWPAKLRLLE GFRNREGLAW SAPRLHLVDL QYSDVRLDKG LYNRLVARGS MERLVTEQQV
LDAVTNPPTD TRAYFRGECL RRFGADIAAA SWDSVIFDLG GESLIRIPTL EPLRGTKAHV
GALLDSVDSA AELVDQLTH
