ID   PUP_MYCA9               Reviewed;          64 AA.
AC   B1MAI1;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=MAB_2171;
OS   Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS   13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacteroides; Mycobacteroides abscessus.
OX   NCBI_TaxID=561007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC   1543;
RX   PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA   Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA   Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA   Gaillard J.L.;
RT   "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT   Mycobacterium abscessus.";
RL   PLoS ONE 4:E5660-E5660(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; CU458896; CAM62252.1; -; Genomic_DNA.
DR   RefSeq; WP_005061283.1; NZ_MLCG01000002.1.
DR   AlphaFoldDB; B1MAI1; -.
DR   SMR; B1MAI1; -.
DR   EnsemblBacteria; CAM62252; CAM62252; MAB_2171.
DR   GeneID; 66972542; -.
DR   KEGG; mab:MAB_2171; -.
DR   OMA; AGQERME; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000007137; 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..64
FT                   /note="Prokaryotic ubiquitin-like protein Pup"
FT                   /id="PRO_0000390586"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          21..58
FT                   /note="ARC ATPase binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   COILED          24..52
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   COMPBIAS        8..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         64
FT                   /note="Deamidated glutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   CROSSLNK        64
FT                   /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT                   with K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
SQ   SEQUENCE   64 AA;  6982 MW;  AD938776C5BC2E2D CRC64;
     MAQEQTKRGG GGDDDDVTDL GGPAGQERRE KLAEDTDDLL DEIDDVLEEN AEDFVRAYVQ
     KGGQ