ID   PUP_BIFAA               Reviewed;          63 AA.
AC   P0CG91;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Prokaryotic ubiquitin-like protein Pup;
DE   AltName: Full=Bacterial ubiquitin-like modifier;
GN   Name=pup; OrderedLocusNames=BAD_0548.1;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) 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 (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
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 ring
CC       (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein family.
CC       {ECO:0000305}.
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DR   EMBL; AP009256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_021913941.1; NC_008618.1.
DR   AlphaFoldDB; P0CG91; -.
DR   SMR; P0CG91; -.
DR   STRING; 1680.BADO_0562; -.
DR   GeneID; 56674632; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000008702; 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_0000395995"
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:0000250"
FT   CROSSLNK        63
FT                   /note="Isoglutamyl lysine isopeptide (Glu-Lys) (interchain
FT                   with K-? in acceptor proteins)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   63 AA;  6931 MW;  E76F0238EEB28485 CRC64;
     MPQKFEQMQS AEQKHDEDET IAQAGTQIDD TVDALDAVLD DIESVLESNA EEYVGSFVQK
     GGE