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PSB_NATMM
ID   PSB_NATMM               Reviewed;         243 AA.
AC   D3SSQ6;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Proteasome subunit beta {ECO:0000255|HAMAP-Rule:MF_02113};
DE            EC=3.4.25.1 {ECO:0000255|HAMAP-Rule:MF_02113};
DE   AltName: Full=20S proteasome beta subunit {ECO:0000255|HAMAP-Rule:MF_02113};
DE   AltName: Full=Proteasome core protein PsmB {ECO:0000255|HAMAP-Rule:MF_02113};
DE   Flags: Precursor;
GN   Name=psmB {ECO:0000255|HAMAP-Rule:MF_02113}; OrderedLocusNames=Nmag_3351;
OS   Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS   IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS   magadii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=547559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861
RC   / NBRC 102185 / NCIMB 2190 / MS3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E.,
RA   Maupin-Furlow J.A., Woyke T.;
RT   "Complete sequence of chromosome of Natrialba magadii ATCC 43099.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the proteasome core, a large protease complex
CC       with broad specificity involved in protein degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_02113}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1; Evidence={ECO:0000255|HAMAP-Rule:MF_02113};
CC   -!- ACTIVITY REGULATION: The formation of the proteasomal ATPase PAN-20S
CC       proteasome complex, via the docking of the C-termini of PAN into the
CC       intersubunit pockets in the alpha-rings, triggers opening of the gate
CC       for substrate entry. Interconversion between the open-gate and close-
CC       gate conformations leads to a dynamic regulation of the 20S proteasome
CC       proteolysis activity. {ECO:0000255|HAMAP-Rule:MF_02113}.
CC   -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14 beta
CC       subunits that assemble into four stacked heptameric rings, resulting in
CC       a barrel-shaped structure. The two inner rings, each composed of seven
CC       catalytic beta subunits, are sandwiched by two outer rings, each
CC       composed of seven alpha subunits. The catalytic chamber with the active
CC       sites is on the inside of the barrel. Has a gated structure, the ends
CC       of the cylinder being occluded by the N-termini of the alpha-subunits.
CC       Is capped at one or both ends by the proteasome regulatory ATPase, PAN.
CC       {ECO:0000255|HAMAP-Rule:MF_02113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|HAMAP-
CC       Rule:MF_02113}.
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DR   EMBL; CP001932; ADD06901.1; -; Genomic_DNA.
DR   RefSeq; WP_004215863.1; NZ_AOHS01000042.1.
DR   AlphaFoldDB; D3SSQ6; -.
DR   SMR; D3SSQ6; -.
DR   STRING; 547559.Nmag_3351; -.
DR   MEROPS; T01.002; -.
DR   EnsemblBacteria; ADD06901; ADD06901; Nmag_3351.
DR   GeneID; 8826217; -.
DR   KEGG; nmg:Nmag_3351; -.
DR   eggNOG; arCOG00970; Archaea.
DR   HOGENOM; CLU_035750_7_2_2; -.
DR   OMA; VDKTGPH; -.
DR   OrthoDB; 89767at2157; -.
DR   Proteomes; UP000001879; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_02113_A; Proteasome_B_A; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR019983; Pept_T1A_Psome_bsu_arc.
DR   InterPro; IPR000243; Pept_T1A_subB.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR03634; arc_protsome_B; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Cytoplasm; Hydrolase; Protease; Proteasome;
KW   Reference proteome; Threonine protease; Zymogen.
FT   PROPEP          1..48
FT                   /note="Removed in mature form; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT                   /id="PRO_0000397382"
FT   CHAIN           49..243
FT                   /note="Proteasome subunit beta"
FT                   /id="PRO_0000397383"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        49
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ   SEQUENCE   243 AA;  25850 MW;  15DDE77BF93C6CAF CRC64;
     MRAPQHNSDF SRTVNQLADD PNPYEPEVGS MPKNEFSRAD LDNVNKTGTT TIGITTEDGV
     VIATDMRASL GGRFVSNKNV QKVEQIHPTG ALTMVGSVGG AQSFIGSLRA EVNLYEARRG
     EPISMDALAT LAGNFARGGP FFAIHPILGG VDEEGSHVYS IDPAGGVMED DYTVTGSGMQ
     LAYGLLEQEF EEDLSNDEAT TVAARAIKSA AERDTGSGNG VFLCEITDEG VDIHGHHDFD
     EVV
 
 
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