ID   A0A1I0UF01_9NOCA        Unreviewed;        63 AA.
AC   A0A1I0UF01;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   20-DEC-2017, entry version 5.
DE   RecName: Full=Prokaryotic ubiquitin-like protein Pup {ECO:0000256|HAMAP-Rule:MF_02106};
DE   AltName: Full=Bacterial ubiquitin-like modifier {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; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   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
CC       proteasomal degradation. The tagging system is termed pupylation.
CC       {ECO:0000256|HAMAP-Rule:MF_02106, ECO:0000256|SAAS:SAAS00276152}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_02106, ECO:0000256|SAAS:SAAS00373196}.
CC   -!- SUBUNIT: Strongly interacts with the proteasome-associated ATPase
CC       ARC through a hydrophobic interface; the interacting region of Pup
CC       lies in its C-terminal half. There is one Pup binding site per ARC
CC       hexamer 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
CC       but is not needed for pupylation, while the C-terminal helical
CC       half of Pup interacts with ARC to target proteins to the
CC       proteasome. {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
CC       family. {ECO:0000256|HAMAP-Rule:MF_02106,
CC       ECO:0000256|SAAS:SAAS00562934}.
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DR   EMBL; FOJN01000024; SFA62615.1; -; Genomic_DNA.
DR   RefSeq; WP_068101305.1; NZ_LPZO01000064.1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000182054};
KW   Isopeptide bond {ECO:0000256|HAMAP-Rule:MF_02106};
KW   Ubl conjugation pathway {ECO:0000256|HAMAP-Rule:MF_02106}.
FT   REGION       20     57       ARC ATPase binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_02106}.
FT   COILED       28     48       {ECO:0000256|SAM:Coils}.
FT   MOD_RES      63     63       Deamidated glutamine. {ECO:0000256|HAMAP-
FT                                Rule:MF_02106}.
FT   CROSSLNK     63     63       Isoglutamyl lysine isopeptide (Gln-Lys)
FT                                (interchain with K-? in acceptor
FT                                proteins). {ECO:0000256|HAMAP-Rule:
FT                                MF_02106}.
SQ   SEQUENCE   63 AA;  6832 MW;  E024CC5C8ED92A56 CRC64;
     MAQEQTTRSG GGDDDEGGAE GASGQERREK LAEETDDLLD EIDDVLEENA EDFVRAYVQK
     GGQ
//