ID   BPA_MYCBO               Reviewed;         174 AA.
AC   P65092; A0A1R3Y592; P72046; X2BQ23;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Bacterial proteasome activator {ECO:0000250|UniProtKB:P9WKX3};
GN   Name=bpa; OrderedLocusNames=BQ2027_MB3809;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=SIU02438.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; LT708304; SIU02438.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_857446.1; NC_002945.3.
DR   AlphaFoldDB; P65092; -.
DR   SMR; P65092; -.
DR   EnsemblBacteria; SIU02438; SIU02438; BQ2027_MB3809.
DR   PATRIC; fig|233413.5.peg.4166; -.
DR   Proteomes; UP000001419; 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_0000104146"
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