ID   PUP_STRCO               Reviewed;          72 AA.
AC   Q7AKQ4; O87596;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=SCO1646;
GN   ORFNames=SCI41.29c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=9765579; DOI=10.1128/jb.180.20.5448-5453.1998;
RA   Nagy I., Tamura T., Vanderleyden J., Baumeister W., De Mot R.;
RT   "The 20S proteasome of Streptomyces coelicolor.";
RL   J. Bacteriol. 180:5448-5453(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(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.
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; AF086832; AAC64276.1; -; Genomic_DNA.
DR   EMBL; AL939109; CAB59499.1; -; Genomic_DNA.
DR   RefSeq; NP_625921.1; NC_003888.3.
DR   RefSeq; WP_011027899.1; NZ_VNID01000018.1.
DR   AlphaFoldDB; Q7AKQ4; -.
DR   SMR; Q7AKQ4; -.
DR   STRING; 100226.SCO1646; -.
DR   GeneID; 1097077; -.
DR   KEGG; sco:SCO1646; -.
DR   PATRIC; fig|100226.15.peg.1660; -.
DR   eggNOG; ENOG50333JS; Bacteria.
DR   HOGENOM; CLU_183816_2_0_11; -.
DR   InParanoid; Q7AKQ4; -.
DR   OMA; DTGGQKH; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000001973; 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..72
FT                   /note="Prokaryotic ubiquitin-like protein Pup"
FT                   /id="PRO_0000390614"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          28..66
FT                   /note="ARC ATPase binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   COILED          10..60
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   COMPBIAS        15..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        72
FT                   /note="Isoglutamyl lysine isopeptide (Glu-Lys) (interchain
FT                   with K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
SQ   SEQUENCE   72 AA;  7976 MW;  03BF8ECE99843464 CRC64;
     MATKDTGGGQ QKATRSTEEV EEQAQDAQAS EDLKERQEKL SDDVDSVLDE IDDVLEENAE
     DFVRSFVQKG GE