ID   PUP_CORGL               Reviewed;          64 AA.
AC   Q8NQE0; Q6M589;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 94.
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};
GN   OrderedLocusNames=Cgl1495, cg1689;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [3]
RP   FUNCTION, INTERACTION WITH PAFA AND DOP, AND DOMAIN.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=22910360; DOI=10.1038/ncomms2009;
RA   Ozcelik D., Barandun J., Schmitz N., Sutter M., Guth E., Damberger F.F.,
RA   Allain F.H., Ban N., Weber-Ban E.;
RT   "Structures of Pup ligase PafA and depupylase Dop from the prokaryotic
RT   ubiquitin-like modification pathway.";
RL   Nat. Commun. 3:1014-1014(2012).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 38-64 IN COMPLEX WITH PROTEIN
RP   PAFA, AND INTERACTION WITH PAFA.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=23601177; DOI=10.1021/ja4024012;
RA   Barandun J., Delley C.L., Ban N., Weber-Ban E.;
RT   "Crystal structure of the complex between prokaryotic ubiquitin-like
RT   protein and its ligase PafA.";
RL   J. Am. Chem. Soc. 135:6794-6797(2013).
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, ECO:0000269|PubMed:22910360}.
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 ring
CC       (By similarity). Interacts with the Pup--protein ligase PafA and with
CC       the depupylase Dop via its C-terminal half. {ECO:0000255|HAMAP-
CC       Rule:MF_02106, ECO:0000269|PubMed:22910360,
CC       ECO:0000269|PubMed:23601177}.
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 (By
CC       similarity). The C-terminal 26 residues of PuP also interact with PafA
CC       and Dop. {ECO:0000255|HAMAP-Rule:MF_02106,
CC       ECO:0000269|PubMed:22910360}.
CC   -!- SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_02106}.
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DR   EMBL; BA000036; BAB98888.1; -; Genomic_DNA.
DR   EMBL; BX927152; CAF21503.1; -; Genomic_DNA.
DR   RefSeq; NP_600711.1; NC_003450.3.
DR   RefSeq; WP_003856167.1; NC_006958.1.
DR   PDB; 4BJR; X-ray; 2.80 A; A/B=38-64.
DR   PDBsum; 4BJR; -.
DR   AlphaFoldDB; Q8NQE0; -.
DR   SMR; Q8NQE0; -.
DR   STRING; 196627.cg1689; -.
DR   GeneID; 58309313; -.
DR   KEGG; cgb:cg1689; -.
DR   KEGG; cgl:Cgl1495; -.
DR   PATRIC; fig|196627.13.peg.1462; -.
DR   eggNOG; ENOG5033BS6; Bacteria.
DR   HOGENOM; CLU_183816_1_0_11; -.
DR   OMA; AGQERME; -.
DR   BRENDA; 6.3.1.19; 960.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000000582; 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   1: Evidence at protein level;
KW   3D-structure; Isopeptide bond; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..64
FT                   /note="Prokaryotic ubiquitin-like protein Pup"
FT                   /id="PRO_0000390576"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          20..58
FT                   /note="ARC ATPase binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   CROSSLNK        64
FT                   /note="Isoglutamyl lysine isopeptide (Glu-Lys) (interchain
FT                   with K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   HELIX           38..46
FT                   /evidence="ECO:0007829|PDB:4BJR"
FT   HELIX           51..57
FT                   /evidence="ECO:0007829|PDB:4BJR"
SQ   SEQUENCE   64 AA;  6830 MW;  1E40C172468856F6 CRC64;
     MNAKQTQIMG GGGRDEDNAE DSAQASGQVQ INTEGVDSLL DEIDGLLENN AEEFVRSYVQ
     KGGE