PUP_MYCTO
ID PUP_MYCTO Reviewed; 64 AA.
AC P9WHN4; B6DAC1; L0TBK1; O33246; Q7D7I1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Prokaryotic ubiquitin-like protein Pup;
DE AltName: Full=Bacterial ubiquitin-like modifier;
GN Name=pup; OrderedLocusNames=MT2171;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 FabD, PanB and Mpa proteins (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC -!- SUBUNIT: Strongly interacts with the proteasome-associated ATPase ARC
CC (Mpa) through a hydrophobic interface; the interacting region of Pup
CC lies in its C-terminal half. {ECO:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK46454.1; -; Genomic_DNA.
DR PIR; B70512; B70512.
DR RefSeq; WP_003411026.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WHN4; -.
DR SMR; P9WHN4; -.
DR EnsemblBacteria; AAK46454; AAK46454; MT2171.
DR GeneID; 45426086; -.
DR KEGG; mtc:MT2171; -.
DR PATRIC; fig|83331.31.peg.2341; -.
DR HOGENOM; CLU_183816_1_0_11; -.
DR UniPathway; UPA00997; -.
DR Proteomes; UP000001020; 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 Coiled coil.
FT CHAIN 1..64
FT /note="Prokaryotic ubiquitin-like protein Pup"
FT /id="PRO_0000428154"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..58
FT /note="Mpa/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:0000250"
SQ SEQUENCE 64 AA; 6944 MW; 7D958B770D8766E3 CRC64;
MAQEQTKRGG GGGDDDDIAG STAAGQERRE KLTEETDDLL DEIDDVLEEN AEDFVRAYVQ
KGGQ