PUP_CORGB
ID PUP_CORGB Reviewed; 64 AA.
AC A4QE81;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=cgR_1555;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
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 -!- SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein family.
CC {ECO:0000255|HAMAP-Rule:MF_02106}.
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DR EMBL; AP009044; BAF54547.1; -; Genomic_DNA.
DR RefSeq; WP_003856167.1; NC_009342.1.
DR AlphaFoldDB; A4QE81; -.
DR SMR; A4QE81; -.
DR EnsemblBacteria; BAF54547; BAF54547; cgR_1555.
DR GeneID; 58309313; -.
DR KEGG; cgt:cgR_1555; -.
DR HOGENOM; CLU_183816_1_0_11; -.
DR OMA; AGQERME; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000006698; 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 Isopeptide bond; Ubl conjugation pathway.
FT CHAIN 1..64
FT /note="Prokaryotic ubiquitin-like protein Pup"
FT /id="PRO_0000390577"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 20..58
FT /note="ARC ATPase binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT CROSSLNK 64
FT /note="Isoglutamyl lysine isopeptide (Glu-Lys) (interchain
FT with K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
SQ SEQUENCE 64 AA; 6830 MW; 1E40C172468856F6 CRC64;
MNAKQTQIMG GGGRDEDNAE DSAQASGQVQ INTEGVDSLL DEIDGLLENN AEEFVRSYVQ
KGGE
