PUP_BIFDB
ID PUP_BIFDB Reviewed; 63 AA.
AC D2Q9C9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 50.
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=BDP_0754;
OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=401473;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1;
RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT adaptation to the human oral cavity.";
RL PLoS Genet. 5:E1000785-E1000785(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; CP001750; ADB09415.1; -; Genomic_DNA.
DR RefSeq; WP_012902012.1; NC_013714.1.
DR AlphaFoldDB; D2Q9C9; -.
DR SMR; D2Q9C9; -.
DR STRING; 401473.BDP_0754; -.
DR EnsemblBacteria; ADB09415; ADB09415; BDP_0754.
DR GeneID; 31605972; -.
DR KEGG; bde:BDP_0754; -.
DR eggNOG; ENOG5031YAF; Bacteria.
DR HOGENOM; CLU_183816_0_0_11; -.
DR OMA; MPQEFEQ; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000008693; 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; Ubl conjugation pathway.
FT CHAIN 1..63
FT /note="Prokaryotic ubiquitin-like protein Pup"
FT /id="PRO_0000395996"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 19..57
FT /note="ARC ATPase binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT CROSSLNK 63
FT /note="Isoglutamyl lysine isopeptide (Glu-Lys) (interchain
FT with K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
SQ SEQUENCE 63 AA; 6786 MW; E24BCC61C1E5A50C CRC64;
MPQEFEQIRS ADQPLDSEES APVAGARTDD TVDALDAVLD DIESVLETNA EEYVGSFVQK
GGE