PUP_THEFY
ID PUP_THEFY Reviewed; 67 AA.
AC Q47NZ3;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=Tfu_1791;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ55826.1; -; Genomic_DNA.
DR RefSeq; WP_011292217.1; NC_007333.1.
DR AlphaFoldDB; Q47NZ3; -.
DR SMR; Q47NZ3; -.
DR STRING; 269800.Tfu_1791; -.
DR EnsemblBacteria; AAZ55826; AAZ55826; Tfu_1791.
DR KEGG; tfu:Tfu_1791; -.
DR eggNOG; ENOG50333JS; Bacteria.
DR HOGENOM; CLU_183816_2_0_11; -.
DR OMA; DTGGQKH; -.
DR UniPathway; UPA00997; -.
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; Ubl conjugation pathway.
FT CHAIN 1..67
FT /note="Prokaryotic ubiquitin-like protein Pup"
FT /id="PRO_0000390616"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 23..61
FT /note="ARC ATPase binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT COILED 27..55
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT COMPBIAS 8..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 67
FT /note="Isoglutamyl lysine isopeptide (Glu-Lys) (interchain
FT with K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
SQ SEQUENCE 67 AA; 7608 MW; 0D52F854729A2256 CRC64;
MATKETGGQK HATRRNQEVE EIEVTTETSV RNEKLAEDVD DILDEIDEVL ESNAEDFVRQ
FVQKGGE
