ID   A0A1I0UF01_9NOCA        Unreviewed;        63 AA.
AC   A0A1I0UF01;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   03-MAY-2023, entry version 15.
DE   RecName: Full=Prokaryotic ubiquitin-like protein Pup {ECO:0000256|ARBA:ARBA00016748, ECO:0000256|HAMAP-Rule:MF_02106};
DE   AltName: Full=Bacterial ubiquitin-like modifier {ECO:0000256|ARBA:ARBA00032321, ECO:0000256|HAMAP-Rule:MF_02106};
GN   Name=pup {ECO:0000256|HAMAP-Rule:MF_02106};
GN   ORFNames=SAMN05444374_12411 {ECO:0000313|EMBL:SFA62615.1};
OS   Rhodococcus kroppenstedtii.
OC   Bacteria; Actinomycetota; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=293050 {ECO:0000313|EMBL:SFA62615.1, ECO:0000313|Proteomes:UP000182054};
RN   [1] {ECO:0000313|EMBL:SFA62615.1, ECO:0000313|Proteomes:UP000182054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44908 {ECO:0000313|EMBL:SFA62615.1,
RC   ECO:0000313|Proteomes:UP000182054};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_02106}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC       {ECO:0000256|ARBA:ARBA00004707, ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_02106}.
CC   -!- SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein family.
CC       {ECO:0000256|ARBA:ARBA00010616, ECO:0000256|HAMAP-Rule:MF_02106}.
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DR   EMBL; FOJN01000024; SFA62615.1; -; Genomic_DNA.
DR   RefSeq; WP_068101305.1; NZ_LPZO01000064.1.
DR   AlphaFoldDB; A0A1I0UF01; -.
DR   EnsemblBacteria; SFA62615; SFA62615; SAMN05444374_12411.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000182054; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_02106};
KW   Ubl conjugation pathway {ECO:0000256|HAMAP-Rule:MF_02106}.
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:0000256|HAMAP-Rule:MF_02106"
FT   COMPBIAS        9..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:0000256|HAMAP-Rule:MF_02106"
FT   CROSSLNK        63
FT                   /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT                   with K-? in acceptor proteins)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02106"
SQ   SEQUENCE   63 AA;  6832 MW;  E024CC5C8ED92A56 CRC64;
     MAQEQTTRSG GGDDDEGGAE GASGQERREK LAEETDDLLD EIDDVLEENA EDFVRAYVQK
     GGQ
//