PUP_MYCLB
ID PUP_MYCLB Reviewed; 63 AA.
AC B8ZRF2;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 55.
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=MLBr01321;
OS Mycobacterium leprae (strain Br4923).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=561304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Br4923;
RX PubMed=19881526; DOI=10.1038/ng.477;
RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA Rougemont J., Brennan P.J., Cole S.T.;
RT "Comparative genomic and phylogeographic analysis of Mycobacterium
RT leprae.";
RL Nat. Genet. 41:1282-1289(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 -!- 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: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; FM211192; CAR71416.1; -; Genomic_DNA.
DR RefSeq; WP_010908270.1; NC_011896.1.
DR AlphaFoldDB; B8ZRF2; -.
DR SMR; B8ZRF2; -.
DR EnsemblBacteria; CAR71416; CAR71416; MLBr01321.
DR KEGG; mlb:MLBr01321; -.
DR HOGENOM; CLU_183816_1_0_11; -.
DR OMA; AGQERME; -.
DR OrthoDB; 2059180at2; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000006900; 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; Ubl conjugation pathway.
FT CHAIN 1..63
FT /note="Prokaryotic ubiquitin-like protein Pup"
FT /id="PRO_0000390593"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 20..57
FT /note="ARC ATPase binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT COILED 23..51
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT COMPBIAS 8..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT CROSSLNK 63
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
SQ SEQUENCE 63 AA; 7067 MW; 0C12293588D92281 CRC64;
MAQEQTRRGG GGDDDEFTSS TSVGQERREK LTEETDDLLD EIDDVLEENA EDFVRAYVQK
GGQ