ID   PUP_ACIC1               Reviewed;          71 AA.
AC   A0LU49;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=Acel_1187;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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; CP000481; ABK52959.1; -; Genomic_DNA.
DR   RefSeq; WP_011720022.1; NC_008578.1.
DR   PDB; 7OXY; X-ray; 1.65 A; B=44-71.
DR   PDB; 7OY3; X-ray; 1.78 A; B=44-71.
DR   PDB; 7OYF; X-ray; 1.88 A; B=44-71.
DR   PDB; 7OYH; X-ray; 1.75 A; B=44-71.
DR   PDBsum; 7OXY; -.
DR   PDBsum; 7OY3; -.
DR   PDBsum; 7OYF; -.
DR   PDBsum; 7OYH; -.
DR   AlphaFoldDB; A0LU49; -.
DR   SMR; A0LU49; -.
DR   STRING; 351607.Acel_1187; -.
DR   EnsemblBacteria; ABK52959; ABK52959; Acel_1187.
DR   KEGG; ace:Acel_1187; -.
DR   eggNOG; ENOG50333JS; Bacteria.
DR   HOGENOM; CLU_183816_2_0_11; -.
DR   OMA; DTGGQKH; -.
DR   OrthoDB; 2059180at2; -.
DR   BRENDA; 3.5.1.119; 9545.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000008221; 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   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Isopeptide bond; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..71
FT                   /note="Prokaryotic ubiquitin-like protein Pup"
FT                   /id="PRO_0000390567"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          27..65
FT                   /note="ARC ATPase binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   COILED          30..59
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   CROSSLNK        71
FT                   /note="Isoglutamyl lysine isopeptide (Glu-Lys) (interchain
FT                   with K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   HELIX           45..53
FT                   /evidence="ECO:0007829|PDB:7OXY"
FT   HELIX           58..64
FT                   /evidence="ECO:0007829|PDB:7OXY"
SQ   SEQUENCE   71 AA;  8105 MW;  71CEAD87C60CCBC0 CRC64;
     MPEKDTGGQH RATRRTEEHD ETIDEATATS DVQERREKLD ADVDAILDEI DDVLEENAEE
     FVRSYIQKGG E