ID   PSB_HALVD               Reviewed;         243 AA.
AC   D4GYZ1; Q9V2V4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
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};
GN   OrderedLocusNames=HVO_1562;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 50-79, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   ACTIVITY REGULATION, SALT REQUIREMENT, AND SUBUNIT.
RX   PubMed=10482525; DOI=10.1128/jb.181.18.5814-5824.1999;
RA   Wilson H.L., Aldrich H.C., Maupin-Furlow J.;
RT   "Halophilic 20S proteasomes of the archaeon Haloferax volcanii:
RT   purification, characterization, and gene sequence analysis.";
RL   J. Bacteriol. 181:5814-5824(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC   VKM B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [3]
RP   SUBUNIT.
RX   PubMed=12486053; DOI=10.1128/jb.185.1.165-174.2003;
RA   Kaczowka S.J., Maupin-Furlow J.A.;
RT   "Subunit topology of two 20S proteasomes from Haloferax volcanii.";
RL   J. Bacteriol. 185:165-174(2003).
RN   [4]
RP   INDUCTION.
RX   PubMed=15516591; DOI=10.1128/jb.186.22.7763-7772.2004;
RA   Reuter C.J., Kaczowka S.J., Maupin-Furlow J.A.;
RT   "Differential regulation of the PanA and PanB proteasome-activating
RT   nucleotidase and 20S proteasomal proteins of the haloarchaeon Haloferax
RT   volcanii.";
RL   J. Bacteriol. 186:7763-7772(2004).
RN   [5]
RP   PHOSPHORYLATION AT SER-129.
RX   PubMed=16950923; DOI=10.1128/jb.00943-06;
RA   Humbard M.A., Stevens S.M. Jr., Maupin-Furlow J.A.;
RT   "Posttranslational modification of the 20S proteasomal proteins of the
RT   archaeon Haloferax volcanii.";
RL   J. Bacteriol. 188:7521-7530(2006).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18931121; DOI=10.1128/jb.01180-08;
RA   Zhou G., Kowalczyk D., Humbard M.A., Rohatgi S., Maupin-Furlow J.A.;
RT   "Proteasomal components required for cell growth and stress responses in
RT   the haloarchaeon Haloferax volcanii.";
RL   J. Bacteriol. 190:8096-8105(2008).
CC   -!- FUNCTION: Component of the proteasome core, a large protease complex
CC       with broad specificity involved in protein degradation. The H.volcanii
CC       alpha1-beta proteasome is able to cleave oligopeptides after Phe, Tyr
CC       and Trp, poorly after Glu but not after Arg. Thus, displays
CC       chymotrypsin-like activity, low caspase-like activity but no trypsin-
CC       like activity. {ECO:0000255|HAMAP-Rule:MF_02113,
CC       ECO:0000269|PubMed:10482525}.
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         ECO:0000269|PubMed:10482525};
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 (By similarity). In vitro, the chymotrypsin-like
CC       activity of the alpha1-beta proteasome is potently inhibited by
CC       carbobenzoxyl-leucinyl-leucinyl-leucinal-H (MG132) and significantly by
CC       N-acetyl-leucinyl-leucinyl-norleucinal-H (calpain inhibitor I).
CC       {ECO:0000255|HAMAP-Rule:MF_02113, ECO:0000269|PubMed:10482525}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0-9.3 for the Suc-LLVY-Amc hydrolyzing activity (with
CC         the alpha1-beta proteasome subtype). {ECO:0000269|PubMed:10482525};
CC       Temperature dependence:
CC         Optimum temperature is 75 degrees Celsius for the Suc-LLVY-Amc
CC         hydrolyzing activity (with the alpha1-beta proteasome subtype).
CC         {ECO:0000269|PubMed:10482525};
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. H.volcanii produces at least 2 types
CC       of 20S proteasomes: an alpha1-beta proteasome and a proteasome
CC       containing all three subunits (alpha1, alpha2, and beta) that appears
CC       to be asymmetrical with homo-oligomeric alpha1 and alpha2 rings
CC       positioned on separate ends. The catalytic chamber with the active
CC       sites is on the inside of the barrel. Has probably a gated structure,
CC       the ends of the cylinder being occluded by the N-termini of the alpha-
CC       subunits. Is likely capped at one or both ends by the proteasome
CC       regulatory ATPase, PAN. {ECO:0000269|PubMed:10482525,
CC       ECO:0000269|PubMed:12486053}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}.
CC   -!- INDUCTION: Up-regulated at the mRNA level during transition from
CC       exponential to stationary phase. However, at the protein level, PsmB is
CC       expressed at a high and relatively constant level throughout growth.
CC       {ECO:0000269|PubMed:15516591}.
CC   -!- DISRUPTION PHENOTYPE: Strains lacking psmB gene are inviable.
CC       {ECO:0000269|PubMed:18931121}.
CC   -!- MISCELLANEOUS: H.volcanii proteasome requires high concentrations of
CC       salt, similar to the extracellular environment and cytoplasm of this
CC       organism, for complex stability and optimal activity.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|HAMAP-
CC       Rule:MF_02113}.
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DR   EMBL; AF126262; AAD53406.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE03141.1; -; Genomic_DNA.
DR   PIR; T48677; T48677.
DR   RefSeq; WP_004041440.1; NZ_AOHU01000028.1.
DR   AlphaFoldDB; D4GYZ1; -.
DR   SMR; D4GYZ1; -.
DR   STRING; 309800.HVO_1562; -.
DR   MEROPS; T01.002; -.
DR   iPTMnet; D4GYZ1; -.
DR   PaxDb; 309800-C498_03165; -.
DR   EnsemblBacteria; ADE03141; ADE03141; HVO_1562.
DR   GeneID; 8923965; -.
DR   KEGG; hvo:HVO_1562; -.
DR   eggNOG; arCOG00970; Archaea.
DR   HOGENOM; CLU_035750_7_2_2; -.
DR   OrthoDB; 6330at2157; -.
DR   Proteomes; UP000008243; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:UniProtKB.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB.
DR   CDD; cd03764; proteasome_beta_archeal; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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   NCBIfam; TIGR03634; arc_protsome_B; 1.
DR   PANTHER; PTHR32194:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1.
DR   PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Phosphoprotein; Protease; Proteasome; Reference proteome;
KW   Threonine protease; Zymogen.
FT   PROPEP          1..49
FT                   /note="Removed in mature form; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02113,
FT                   ECO:0000269|PubMed:10482525"
FT                   /id="PRO_0000397605"
FT   CHAIN           50..243
FT                   /note="Proteasome subunit beta"
FT                   /id="PRO_0000397606"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        50
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16950923"
SQ   SEQUENCE   243 AA;  25994 MW;  6253E28ADDA40E61 CRC64;
     MRTPTHDEFS GRLDSLNGDR SNVFGPELGE FSNADRRADE LGDKETKTGT TTVGIKTEEG
     VVLATDMRAS MGYMVSSKDV QKVEEIHPTG ALTIAGSVSA AQSLISSLRA EVRLYEARRG
     EDMSMQALST LVGNFLRSGG FYVVQPILGG VDETGPHIYS IDPAGSILEE EYTVTGSGSQ
     YALGVLEQEF EDGLSIEEAK GVATKAIRSA VERDLASGNG INIAVVTEDG VDIQRHQNFE
     GLE
//