ID   PUP_BIFLO               Reviewed;          67 AA.
AC   P0CG92;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Prokaryotic ubiquitin-like protein Pup;
DE   AltName: Full=Bacterial ubiquitin-like modifier;
GN   Name=pup; OrderedLocusNames=BL1796.1;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_007057184.1; NC_004307.2.
DR   AlphaFoldDB; P0CG92; -.
DR   SMR; P0CG92; -.
DR   STRING; 216816.GS08_07750; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000000439; 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..67
FT                   /note="Prokaryotic ubiquitin-like protein Pup"
FT                   /id="PRO_0000395997"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          23..61
FT                   /note="ARC ATPase binding"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        67
FT                   /note="Isoglutamyl lysine isopeptide (Glu-Lys) (interchain
FT                   with K-? in acceptor proteins)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   67 AA;  7261 MW;  CFD4DB99F13E0EA1 CRC64;
     MPQQFEQPQA QQAATQEDDA LATTQAAAQT ESTDQADVLD DILDDIESAL ETNAEEYVNS
     FVQKGGE