ID   PUP_BRAFD               Reviewed;          62 AA.
AC   C7MCY8;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=Bfae_16180;
OS   Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG
OS   19847 / NBRC 14762 / NCIMB 9860 / 6-10).
OC   Bacteria; Actinobacteria; Micrococcales; Dermabacteraceae; Brachybacterium.
OX   NCBI_TaxID=446465;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 / NCIMB
RC   9860 / 6-10;
RX   PubMed=21304631; DOI=10.4056/sigs.492;
RA   Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A.,
RA   Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Brachybacterium faecium type strain
RT   (Schefferle 6-10).";
RL   Stand. Genomic Sci. 1:3-11(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; CP001643; ACU85445.1; -; Genomic_DNA.
DR   RefSeq; WP_015775654.1; NC_013172.1.
DR   RefSeq; YP_003155035.1; NC_013172.1.
DR   AlphaFoldDB; C7MCY8; -.
DR   SMR; C7MCY8; -.
DR   STRING; 446465.Bfae_16180; -.
DR   EnsemblBacteria; ACU85445; ACU85445; Bfae_16180.
DR   KEGG; bfa:Bfae_16180; -.
DR   PATRIC; fig|446465.5.peg.1611; -.
DR   eggNOG; ENOG5033A24; Bacteria.
DR   HOGENOM; CLU_183816_1_0_11; -.
DR   OMA; MPQEFEQ; -.
DR   OrthoDB; 2059180at2; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000001919; 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   Isopeptide bond; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..62
FT                   /note="Prokaryotic ubiquitin-like protein Pup"
FT                   /id="PRO_0000395998"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          21..56
FT                   /note="ARC ATPase binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   MOD_RES         62
FT                   /note="Deamidated glutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
FT   CROSSLNK        62
FT                   /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT                   with K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02106"
SQ   SEQUENCE   62 AA;  6370 MW;  816A7032303A501B CRC64;
     MSQQSLNAPG PGAEDGNDPE AVTGGQTFAS AQAADDLLDE IDSVLESNAE TFVRSFVQKG
     GQ