ID   BPA_MYCTO               Reviewed;         174 AA.
AC   P9WKX2; L0TDS4; P65091; P72046;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Bacterial proteasome activator {ECO:0000250|UniProtKB:P9WKX3};
GN   Name=bpa; OrderedLocusNames=MT3889;
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: 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. Can inhibit
CC       degradation of Pup-tagged substrates in vitro by competing with Mpa for
CC       association with the proteasome. {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; AE000516; AAK48254.1; -; Genomic_DNA.
DR   PIR; H70695; H70695.
DR   AlphaFoldDB; P9WKX2; -.
DR   SMR; P9WKX2; -.
DR   EnsemblBacteria; AAK48254; AAK48254; MT3889.
DR   KEGG; mtc:MT3889; -.
DR   HOGENOM; CLU_111456_0_0_11; -.
DR   Proteomes; UP000001020; 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.
FT   CHAIN           1..174
FT                   /note="Bacterial proteasome activator"
FT                   /id="PRO_0000427579"
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"
SQ   SEQUENCE   174 AA;  18944 MW;  1A7D60E1A4F3713E CRC64;
     MVIGLSTGSD DDDVEVIGGV DPRLIAVQEN DSDESSLTDL VEQPAKVMRI GTMIKQLLEE
     VRAAPLDEAS RNRLRDIHAT SIRELEDGLA PELREELDRL TLPFNEDAVP SDAELRIAQA
     QLVGWLEGLF HGIQTALFAQ QMAARAQLQQ MRQGALPPGV GKSGQHGHGT GQYL