ID   PUP_MYCSK               Reviewed;          64 AA.
AC   A1UHS8;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=Mkms_3192;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) 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: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; CP000518; ABL92386.1; -; Genomic_DNA.
DR   RefSeq; WP_011768278.1; NC_008705.1.
DR   AlphaFoldDB; A1UHS8; -.
DR   SMR; A1UHS8; -.
DR   STRING; 189918.Mkms_3192; -.
DR   EnsemblBacteria; ABL92386; ABL92386; Mkms_3192.
DR   KEGG; mkm:Mkms_3192; -.
DR   HOGENOM; CLU_183816_1_0_11; -.
DR   OMA; AGQERME; -.
DR   UniPathway; UPA00997; -.
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_0000390597"
FT   REGION          1..37
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        21..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;  6870 MW;  3274BC3FF9A8A038 CRC64;
     MAQEQTKRGG GGGEDDDLSG GAGAGQERRE KLAEETDDLL DEIDDVLEEN AEDFVRAYVQ
     KGGQ