PSB2_SACS2
ID PSB2_SACS2 Reviewed; 208 AA.
AC Q9UXF3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Proteasome subunit beta 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_02113};
DE AltName: Full=Proteasome core protein PsmB 2 {ECO:0000255|HAMAP-Rule:MF_02113};
DE Flags: Precursor;
GN Name=psmB2 {ECO:0000255|HAMAP-Rule:MF_02113}; OrderedLocusNames=SSO0766;
GN ORFNames=C40_002;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK41063.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB57537.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y18930; CAB57537.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006641; AAK41063.1; ALT_INIT; Genomic_DNA.
DR PIR; H90225; H90225.
DR AlphaFoldDB; Q9UXF3; -.
DR SMR; Q9UXF3; -.
DR STRING; 273057.SSO0766; -.
DR MEROPS; T01.002; -.
DR EnsemblBacteria; AAK41063; AAK41063; SSO0766.
DR KEGG; sso:SSO0766; -.
DR PATRIC; fig|273057.12.peg.765; -.
DR eggNOG; arCOG00970; Archaea.
DR HOGENOM; CLU_035750_7_2_2; -.
DR InParanoid; Q9UXF3; -.
DR OMA; VDKTGPH; -.
DR PhylomeDB; Q9UXF3; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR CDD; cd03764; proteasome_beta_archeal; 1.
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; IPR016050; Proteasome_bsu_CS.
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; PS00854; PROTEASOME_BETA_1; 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..14
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT /id="PRO_0000026673"
FT CHAIN 15..208
FT /note="Proteasome subunit beta 2"
FT /id="PRO_0000026674"
FT ACT_SITE 15
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ SEQUENCE 208 AA; 22927 MW; C940A8273AB25CB9 CRC64;
MGNELQLENK ILKGTTTVGI RVNDGVILAA DRRASAGFFV ANKMVRKVLY ITDKIGITTA
GSVADLQFIY DVLKNIYHYN SITKYGPISI KGIATRLANV LSATKYFPYI VQILIGGYDD
QPRLFNLDYL GDITEENYVA TGSGSPVAMG VLEDEYNPKM TLDEAADLAK RAVFSAIKRD
SFTGTGVIVA KIHSKGHEEL EFYLNKKM
