ID   BPA_MYCLE               Reviewed;         174 AA.
AC   Q9CD99;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Bacterial proteasome activator {ECO:0000250|UniProtKB:P9WKX3};
GN   Name=bpa; OrderedLocusNames=ML0115;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Interacts with the core proteasome alpha-subunit (PrcA)
CC       through its C-terminal hydrophobic-tyrosine-X motif (HbYX motif).
CC       Interaction of Bpa with the proteasome stimulates proteosomal peptidase
CC       and casein degradation activity, which suggests Bpa could play a role
CC       in the removal of non-native or damaged proteins by influencing the
CC       conformation of the proteasome complex upon interaction.
CC       {ECO:0000250|UniProtKB:P9WKX3}.
CC   -!- SUBUNIT: Forms a homooligomeric, either hexameric or heptameric, ring-
CC       like structure which stacks co-axially with the proteasomal alpha-
CC       rings. {ECO:0000250|UniProtKB:P9WKX3}.
CC   -!- SIMILARITY: Belongs to the Bpa family. {ECO:0000305}.
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DR   EMBL; AL583917; CAC29623.1; -; Genomic_DNA.
DR   PIR; C86923; C86923.
DR   RefSeq; NP_301211.1; NC_002677.1.
DR   AlphaFoldDB; Q9CD99; -.
DR   SMR; Q9CD99; -.
DR   STRING; 272631.ML0115; -.
DR   EnsemblBacteria; CAC29623; CAC29623; CAC29623.
DR   KEGG; mle:ML0115; -.
DR   PATRIC; fig|272631.5.peg.179; -.
DR   Leproma; ML0115; -.
DR   eggNOG; ENOG502ZPJ4; Bacteria.
DR   HOGENOM; CLU_111456_0_0_11; -.
DR   OMA; TDMVEQP; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:InterPro.
DR   InterPro; IPR019695; Proteasome_act.
DR   Pfam; PF10759; DUF2587; 1.
PE   3: Inferred from homology;
KW   Proteasome; Reference proteome.
FT   CHAIN           1..174
FT                   /note="Bacterial proteasome activator"
FT                   /id="PRO_0000104147"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           172..174
FT                   /note="HbYX motif"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKX3"
FT   COMPBIAS        20..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   174 AA;  19071 MW;  18DF37CD89A96744 CRC64;
     MNNDNDDSIE IIGGVDPRTM ATRGEDESRD SDEPSLTDLV EQPAKVMRIG TMIKQLLEEV
     RAAPLDEASR NQLREIHATS IRELEDGLAP ELREELDRLT LPFNESTAPS NAELRIAQAQ
     LVGWLEGLFH GIQTALFAQQ MAARAQLEQM RHSALPPGMG KPGQAGGQGT GQYL