PUP_COREF
ID PUP_COREF Reviewed; 63 AA.
AC Q8FTE5;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=CE1624;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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; BA000035; BAC18434.1; -; Genomic_DNA.
DR RefSeq; WP_006767624.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8FTE5; -.
DR SMR; Q8FTE5; -.
DR STRING; 196164.23493464; -.
DR EnsemblBacteria; BAC18434; BAC18434; BAC18434.
DR KEGG; cef:CE1624; -.
DR eggNOG; ENOG5033BS6; Bacteria.
DR HOGENOM; CLU_183816_1_0_11; -.
DR OMA; AGQERME; -.
DR OrthoDB; 2059180at2; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000001409; 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; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..63
FT /note="Prokaryotic ubiquitin-like protein Pup"
FT /id="PRO_0000390575"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 19..57
FT /note="ARC ATPase binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT CROSSLNK 63
FT /note="Isoglutamyl lysine isopeptide (Glu-Lys) (interchain
FT with K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
SQ SEQUENCE 63 AA; 6876 MW; 9CA4F3914EDBF1FB CRC64;
MSDRQTQIPA GGGREDDHDD QVQSAGQVQV NTEGVDDLLD EIDGLLENNA EEFVRSYVQK
GGE