DOP_MYCS2
ID DOP_MYCS2 Reviewed; 498 AA.
AC A0QZ49; I7FFQ8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Pup deamidase/depupylase;
DE EC=3.4.-.-;
DE EC=3.5.1.119 {ECO:0000269|PubMed:20025664};
DE AltName: Full=Deamidase of protein Pup;
GN Name=dop; OrderedLocusNames=MSMEG_3897, MSMEI_3807;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION AS PUP DEAMIDASE, CATALYTIC ACTIVITY, ROLE IN THE PROTEASOME
RP DEGRADATION PATHWAY, COFACTOR, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLU-10.
RX PubMed=20025664; DOI=10.1111/j.1365-2958.2009.07013.x;
RA Imkamp F., Rosenberger T., Striebel F., Keller P.M., Amstutz B., Sander P.,
RA Weber-Ban E.;
RT "Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein
RT substrates in vivo.";
RL Mol. Microbiol. 75:744-754(2010).
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. Probably also displays
CC depupylase (DPUP) activity, removing conjugated Pup from target
CC proteins; thus may be 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:0000269|PubMed:20025664}.
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:0000269|PubMed:20025664};
CC -!- COFACTOR:
CC Name=ATP; Xref=ChEBI:CHEBI:30616;
CC Evidence={ECO:0000269|PubMed:20025664};
CC Note=ATP is required for the deamidation reaction but is not hydrolyzed
CC during this reaction. {ECO:0000269|PubMed:20025664};
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC -!- DISRUPTION PHENOTYPE: Pupylation is severely impaired and the steady-
CC state levels of the two known proteasomal substrates FabD and PanB are
CC drastically increased. {ECO:0000269|PubMed:20025664}.
CC -!- MISCELLANEOUS: Is the only enzyme acting as a deamidase of Pup during
CC pupylation.
CC -!- SIMILARITY: Belongs to the Pup ligase/Pup deamidase family. Pup
CC deamidase subfamily. {ECO:0000305}.
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DR EMBL; CP000480; ABK71414.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40265.1; -; Genomic_DNA.
DR RefSeq; WP_003895348.1; NZ_SIJM01000005.1.
DR RefSeq; YP_888187.1; NC_008596.1.
DR AlphaFoldDB; A0QZ49; -.
DR SMR; A0QZ49; -.
DR STRING; 246196.MSMEI_3807; -.
DR PRIDE; A0QZ49; -.
DR EnsemblBacteria; ABK71414; ABK71414; MSMEG_3897.
DR EnsemblBacteria; AFP40265; AFP40265; MSMEI_3807.
DR GeneID; 66735264; -.
DR KEGG; msg:MSMEI_3807; -.
DR KEGG; msm:MSMEG_3897; -.
DR PATRIC; fig|246196.19.peg.3837; -.
DR eggNOG; COG4122; Bacteria.
DR OMA; YFRGRCL; -.
DR OrthoDB; 537546at2; -.
DR BRENDA; 3.5.1.119; 3512.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005524; F:ATP binding; IMP:UniProtKB.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0070490; P:protein pupylation; IMP:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..498
FT /note="Pup deamidase/depupylase"
FT /id="PRO_0000395858"
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:0000305"
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"
FT MUTAGEN 10
FT /note="E->A: Loss of Pup deamidase activity both in vivo
FT and in vitro."
FT /evidence="ECO:0000269|PubMed:20025664"
SQ SEQUENCE 498 AA; 54574 MW; 480A16DAF67AC425 CRC64;
MQRIIGTEVE YGISSPSDPT ANPILTSTQA VLAYAAAAGI QRAKRTRWDY EVESPLRDAR
GFDLSRSSGP PPIVDADEVG AANMILTNGA RLYVDHAHPE YSAPECTDPM DAVIWDKAGE
RVMEAAARHV ASVPGAAKLQ LYKNNVDGKG ASYGSHENYL MSRQTPFSAV IAGLTPFMVS
RQVVTGSGRV GIGPSGDEPG FQLSQRADYI EVEVGLETTL KRGIINTRDE PHADADKYRR
LHVIIGDANL AETSTYLKLG TTSLVLDLIE EGVDLSDLAL ARPVHAVHVI SRDPSLRATV
ALADGRELTA LALQRIYLDR VAKLVDSRDP DPRASHVIET WANVLDLLER DPMECAEILD
WPAKLRLLEG FRQRENLTWQ APRLHLVDLQ YSDVRLDKGL YNRLVARGSM KRLVTEQQVL
DAVENPPTDT RAYFRGECLR RFGADIAAAS WDSVIFDLGG DSLVRIPTLE PLRGSKAHVG
ALLDSVDSAV ELVEQLTN
