ID   PUP_PAEAT               Reviewed;          67 AA.
AC   P0CG90;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Prokaryotic ubiquitin-like protein Pup;
DE   AltName: Full=Bacterial ubiquitin-like modifier;
GN   Name=pup; OrderedLocusNames=AAur_2176.1;
OS   Paenarthrobacter aurescens (strain TC1).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX   NCBI_TaxID=290340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1;
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA   Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT   aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
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   -!- 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:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein family.
CC       {ECO:0000305}.
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DR   EMBL; CP000474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_043806102.1; NC_008711.1.
DR   AlphaFoldDB; P0CG90; -.
DR   SMR; P0CG90; -.
DR   OrthoDB; 2059180at2; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000000637; 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; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..67
FT                   /note="Prokaryotic ubiquitin-like protein Pup"
FT                   /id="PRO_0000395994"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          25..61
FT                   /note="ARC ATPase binding"
FT                   /evidence="ECO:0000250"
FT   COILED          29..49
FT                   /evidence="ECO:0000255"
FT   MOD_RES         67
FT                   /note="Deamidated glutamine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        67
FT                   /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT                   with K-? in acceptor proteins)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   67 AA;  7184 MW;  3B8777E8B35660F0 CRC64;
     MAAQEQQQPQ SRETETEVDV PEAPPAAPEA QASEATQGVD DLLDEIDGVL ESNAEEFVRA
     FVQKGGQ