PUP_RHOOB
ID PUP_RHOOB Reviewed; 64 AA.
AC C1ASP8;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Prokaryotic ubiquitin-like protein Pup {ECO:0000255|HAMAP-Rule:MF_02106};
DE AltName: Full=Bacterial ubiquitin-like modifier {ECO:0000255|HAMAP-Rule:MF_02106};
GN Name=pup {ECO:0000255|HAMAP-Rule:MF_02106}; OrderedLocusNames=ROP_05830;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein modifier that is covalently attached to lysine
CC residues of substrate proteins, thereby targeting them for proteasomal
CC degradation. The tagging system is termed pupylation.
CC {ECO:0000255|HAMAP-Rule:MF_02106}.
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC {ECO:0000255|HAMAP-Rule:MF_02106}.
CC -!- SUBUNIT: Strongly interacts with the proteasome-associated ATPase ARC
CC through a hydrophobic interface; the interacting region of Pup lies in
CC its C-terminal half. There is one Pup binding site per ARC hexamer
CC ring. {ECO:0000255|HAMAP-Rule:MF_02106}.
CC -!- DOMAIN: The N-terminal unstructured half of Pup provides a signal
CC required to initiate unfolding and degradation by the proteasome but is
CC not needed for pupylation, while the C-terminal helical half of Pup
CC interacts with ARC to target proteins to the proteasome.
CC {ECO:0000255|HAMAP-Rule:MF_02106}.
CC -!- PTM: Is modified by deamidation of its C-terminal glutamine to
CC glutamate by the deamidase Dop, a prerequisite to the subsequent
CC pupylation process. {ECO:0000255|HAMAP-Rule:MF_02106}.
CC -!- SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein family.
CC {ECO:0000255|HAMAP-Rule:MF_02106}.
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DR EMBL; AP011115; BAH48830.1; -; Genomic_DNA.
DR RefSeq; WP_005242990.1; NC_012522.1.
DR AlphaFoldDB; C1ASP8; -.
DR SMR; C1ASP8; -.
DR STRING; 632772.ROP_05830; -.
DR EnsemblBacteria; BAH48830; BAH48830; ROP_05830.
DR GeneID; 66787357; -.
DR KEGG; rop:ROP_05830; -.
DR PATRIC; fig|632772.20.peg.641; -.
DR HOGENOM; CLU_183816_1_0_11; -.
DR OMA; AGQERME; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000002212; Chromosome.
DR GO; GO:0070628; F:proteasome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031386; F:protein tag; IEA:UniProtKB-UniRule.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0070490; P:protein pupylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02106; Pup; 1.
DR InterPro; IPR008515; Ubiquitin-like_Pup.
DR Pfam; PF05639; Pup; 1.
DR TIGRFAMs; TIGR03687; pupylate_cterm; 1.
PE 3: Inferred from homology;
KW Coiled coil; Isopeptide bond; Ubl conjugation pathway.
FT CHAIN 1..64
FT /note="Prokaryotic ubiquitin-like protein Pup"
FT /id="PRO_0000390607"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..58
FT /note="ARC ATPase binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT COILED 24..52
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT COMPBIAS 8..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT CROSSLNK 64
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
SQ SEQUENCE 64 AA; 6956 MW; 4A10C854A165702C CRC64;
MAQEQTKRTG GGDEDDTPGG DGAAGQERRE KLAEDTDDLL DEIDDVLEEN AEDFVRAYVQ
KGGQ