BPA_MYCTU
ID BPA_MYCTU Reviewed; 174 AA.
AC P9WKX3; L0TDS4; P65091; P72046;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Bacterial proteasome activator {ECO:0000303|PubMed:25469515};
GN Name=bpa {ECO:0000303|PubMed:25469515}; OrderedLocusNames=Rv3780;
GN ORFNames=MTCY13D12.14;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION, SUBUNIT, INTERACTION WITH PRCA, AND MUTAGENESIS OF
RP 171-GLY--LEU-174.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=25469515; DOI=10.1371/journal.pone.0114348;
RA Delley C.L., Laederach J., Ziemski M., Bolten M., Boehringer D.,
RA Weber-Ban E.;
RT "Bacterial proteasome activator Bpa (Rv3780) is a novel ring-shaped
RT interactor of the mycobacterial proteasome.";
RL PLoS ONE 9:E114348-E114348(2014).
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:0000269|PubMed:25469515}.
CC -!- SUBUNIT: Forms a homooligomeric, either hexameric or heptameric, ring-
CC like structure which stacks co-axially with the proteasomal alpha-
CC rings. {ECO:0000269|PubMed:25469515}.
CC -!- SIMILARITY: Belongs to the Bpa family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP46609.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL123456; CCP46609.1; ALT_INIT; Genomic_DNA.
DR PIR; H70695; H70695.
DR RefSeq; NP_218297.1; NC_000962.3.
DR PDB; 5IET; X-ray; 2.88 A; A/B=15-153.
DR PDB; 5IEU; X-ray; 2.80 A; A/B=44-153.
DR PDB; 5LFJ; X-ray; 2.60 A; A/B/C/D=36-159.
DR PDB; 5LFP; X-ray; 3.30 A; A/B/C/D=36-159.
DR PDB; 5LFQ; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=36-159.
DR PDB; 5LZP; EM; 3.45 A; 1/3/5/7/V/X/Z=2-174.
DR PDB; 6BGL; EM; 3.40 A; B/d/e/f/g/h/i/j/k/l/m/n/o/p=1-174.
DR PDB; 6BGO; EM; 4.20 A; d/e/f/g/h/i/j=1-174.
DR PDBsum; 5IET; -.
DR PDBsum; 5IEU; -.
DR PDBsum; 5LFJ; -.
DR PDBsum; 5LFP; -.
DR PDBsum; 5LFQ; -.
DR PDBsum; 5LZP; -.
DR PDBsum; 6BGL; -.
DR PDBsum; 6BGO; -.
DR AlphaFoldDB; P9WKX3; -.
DR SMR; P9WKX3; -.
DR STRING; 83332.Rv3780; -.
DR PaxDb; P9WKX3; -.
DR DNASU; 886115; -.
DR GeneID; 886115; -.
DR KEGG; mtu:Rv3780; -.
DR PATRIC; fig|83332.12.peg.4211; -.
DR TubercuList; Rv3780; -.
DR eggNOG; ENOG502ZPJ4; Bacteria.
DR OMA; TDMVEQP; -.
DR PHI-base; PHI:4674; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0022624; C:proteasome accessory complex; IDA:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR DisProt; DP01737; -.
DR InterPro; IPR019695; Proteasome_act.
DR Pfam; PF10759; DUF2587; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Proteasome; Reference proteome.
FT CHAIN 1..174
FT /note="Bacterial proteasome activator"
FT /id="PRO_0000104145"
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:0000305|PubMed:25469515"
FT MUTAGEN 171..174
FT /note="Missing: Loss of interaction with the proteasome
FT subunit PrcA."
FT /evidence="ECO:0000269|PubMed:25469515"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:5LFJ"
FT HELIX 44..63
FT /evidence="ECO:0007829|PDB:5LFJ"
FT HELIX 68..87
FT /evidence="ECO:0007829|PDB:5LFJ"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:5LFJ"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5LFP"
FT HELIX 112..144
FT /evidence="ECO:0007829|PDB:5LFJ"
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
