PUP_MYCS2
ID PUP_MYCS2 Reviewed; 64 AA.
AC A0QZ48; I7GCE1; O30517;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Prokaryotic ubiquitin-like protein Pup;
DE AltName: Full=Bacterial ubiquitin-like modifier;
GN Name=pup; Synonyms=prcS; OrderedLocusNames=MSMEG_3896, MSMEI_3806;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9282749; DOI=10.1046/j.1365-2958.1997.4721837.x;
RA Knipfer N., Shrader T.E.;
RT "Inactivation of the 20S proteasome in Mycobacterium smegmatis.";
RL Mol. Microbiol. 25:375-383(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [5]
RP FUNCTION, ROLE IN THE PROTEASOME DEGRADATION PATHWAY, PROTEIN SUBSTRATES,
RP CROSS-LINK SITE TO PROTEASOME SUBSTRATES, DEAMIDATION AT GLN-64, CLEAVAGE
RP OF INITIATOR METHIONINE, MUTAGENESIS OF 62-GLY-GLY-63 AND GLN-64, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19028679; DOI=10.1074/jbc.m808032200;
RA Burns K.E., Liu W.-T., Boshoff H.I.M., Dorrestein P.C., Barry C.E. III;
RT "Proteasomal protein degradation in mycobacteria is dependent upon a
RT prokaryotic ubiquitin-like protein.";
RL J. Biol. Chem. 284:3069-3075(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. Among the
CC identified substrates are the SodA and Ino1 proteins.
CC {ECO:0000269|PubMed:19028679}.
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
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). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- PTM: Is modified by deamidation of its C-terminal glutamine to
CC glutamate probably by the deamidase Dop, a prerequisite to the
CC subsequent pupylation process. {ECO:0000269|PubMed:19028679}.
CC -!- SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein family.
CC {ECO:0000305}.
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DR EMBL; AF009645; AAC45613.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK74855.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40264.1; -; Genomic_DNA.
DR RefSeq; WP_003895347.1; NZ_SIJM01000005.1.
DR RefSeq; YP_888186.1; NC_008596.1.
DR AlphaFoldDB; A0QZ48; -.
DR SMR; A0QZ48; -.
DR STRING; 246196.MSMEI_3806; -.
DR EnsemblBacteria; ABK74855; ABK74855; MSMEG_3896.
DR EnsemblBacteria; AFP40264; AFP40264; MSMEI_3806.
DR GeneID; 66735263; -.
DR KEGG; msg:MSMEI_3806; -.
DR KEGG; msm:MSMEG_3896; -.
DR PATRIC; fig|246196.19.peg.3836; -.
DR eggNOG; ENOG50333JS; Bacteria.
DR OMA; AGQERME; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0070628; F:proteasome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031386; F:protein tag; IDA:UniProtKB.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB.
DR GO; GO:0070490; P:protein pupylation; IDA:UniProtKB.
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 Coiled coil; Isopeptide bond; Reference proteome; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19028679"
FT CHAIN 2..64
FT /note="Prokaryotic ubiquitin-like protein Pup"
FT /id="PRO_0000383477"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..58
FT /note="ARC ATPase binding"
FT /evidence="ECO:0000250"
FT COILED 23..52
FT /evidence="ECO:0000255"
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:0000269|PubMed:19028679"
FT CROSSLNK 64
FT /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT with K-? in acceptor proteins)"
FT MUTAGEN 62..63
FT /note="Missing: Abrogates pupylation of substrate
FT proteins."
FT /evidence="ECO:0000269|PubMed:19028679"
FT MUTAGEN 64
FT /note="Missing: Abrogates pupylation of substrate
FT proteins."
FT /evidence="ECO:0000269|PubMed:19028679"
SQ SEQUENCE 64 AA; 6954 MW; 60383C10BB4F2DE3 CRC64;
MAQEQTKRGG GGGEDDDLPG ASAAGQERRE KLTEETDDLL DEIDDVLEEN AEDFVRAYVQ
KGGQ
