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Database: UniProt
Entry: A0A0Q9LIE0_9MICC
LinkDB: A0A0Q9LIE0_9MICC
Original site: A0A0Q9LIE0_9MICC 
ID   A0A0Q9LIE0_9MICC        Unreviewed;       197 AA.
AC   A0A0Q9LIE0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Bacterial proteasome activator {ECO:0000256|ARBA:ARBA00014831};
GN   ORFNames=ASG92_05660 {ECO:0000313|EMBL:KRE53485.1};
OS   Arthrobacter sp. Soil736.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736395 {ECO:0000313|EMBL:KRE53485.1, ECO:0000313|Proteomes:UP000051775};
RN   [1] {ECO:0000313|Proteomes:UP000051775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil736 {ECO:0000313|Proteomes:UP000051775};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE53485.1, ECO:0000313|Proteomes:UP000051775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil736 {ECO:0000313|EMBL:KRE53485.1,
RC   ECO:0000313|Proteomes:UP000051775};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Forms a homooligomeric, either hexameric or heptameric, ring-
CC       like structure which stacks co-axially with the proteasomal alpha-
CC       rings. {ECO:0000256|ARBA:ARBA00011402}.
CC   -!- SIMILARITY: Belongs to the Bpa family. {ECO:0000256|ARBA:ARBA00006639}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRE53485.1}.
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DR   EMBL; LMSB01000034; KRE53485.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9LIE0; -.
DR   STRING; 1736395.ASG92_05660; -.
DR   OrthoDB; 5189298at2; -.
DR   Proteomes; UP000051775; Unassembled WGS sequence.
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; BPA; 1.
PE   3: Inferred from homology;
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   197 AA;  21182 MW;  F07BADE239A34BAF CRC64;
     MPVEGTTLDG DAVPEDGHTP SEPAKLKRTS LQDLVDEPAK VMRIGTMIRQ LLEEVKAAPL
     DDAARGRLVE IHERSIKELE DGLAPELVAE LERISLPFPD NATPSDAELR IAQAQLVGWL
     EGLFHGIQTA IAAQHAAREQ AMAQMQLRQL PPGTVIAPGV VIGEHGEPQR AKAPQPGADT
     AQPGRKEDSD HGPGQYL
//
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