ID   PSB_HALUD               Reviewed;         234 AA.
AC   C7NQ99;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 54.
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=Huta_2664;
OS   Halorhabdus utahensis (strain DSM 12940 / JCM 11049 / AX-2).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halorhabdus.
OX   NCBI_TaxID=519442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12940 / JCM 11049 / AX-2;
RX   PubMed=21304660; DOI=10.4056/sigs.31864;
RA   Anderson I., Tindall B.J., Pomrenke H., Goker M., Lapidus A., Nolan M.,
RA   Copeland A., Glavina Del Rio T., Chen F., Tice H., Cheng J.F., Lucas S.,
RA   Chertkov O., Bruce D., Brettin T., Detter J.C., Han C., Goodwin L.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Pitluck S., Pati A.,
RA   Mavromatis K., Ivanova N., Ovchinnikova G., Chen A., Palaniappan K.,
RA   Chain P., Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Halorhabdus utahensis type strain (AX-2).";
RL   Stand. Genomic Sci. 1:218-225(2009).
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; CP001687; ACV12825.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7NQ99; -.
DR   SMR; C7NQ99; -.
DR   STRING; 519442.Huta_2664; -.
DR   MEROPS; T01.002; -.
DR   EnsemblBacteria; ACV12825; ACV12825; Huta_2664.
DR   KEGG; hut:Huta_2664; -.
DR   eggNOG; arCOG00970; Archaea.
DR   HOGENOM; CLU_035750_7_2_2; -.
DR   OMA; VDKTGPH; -.
DR   Proteomes; UP000002071; 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   Threonine protease; Zymogen.
FT   PROPEP          1..39
FT                   /note="Removed in mature form; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT                   /id="PRO_0000397306"
FT   CHAIN           40..234
FT                   /note="Proteasome subunit beta"
FT                   /id="PRO_0000397307"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        40
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ   SEQUENCE   234 AA;  24512 MW;  503481AE68C2FC1C CRC64;
     MNPDLNMNPH DSGRTDPYAP ELGEIATDEG DGENVTKTGT TTVGLATEEG VVIATDRRAS
     LGGRFVSNKN VVKVEEIHPT AAMTLVGSVG GAQSFIRTLR SEASLYETRR DEPMSINALA
     TLAGNFARGG PFLAIHPILG GVDDEGSHVY TIDPAGGVME DDYAVTGSGM QVAYGTIEGE
     YESDLSTEEA KELATNAVQA ASERDTGSGN GLVIAEITDE GVEIEEFDDL ADAL