PSB_METJA
ID PSB_METJA Reviewed; 224 AA.
AC Q58634;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 135.
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=MJ1237;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND INTERACTION WITH PAN.
RX PubMed=10692374; DOI=10.1128/jb.182.6.1680-1692.2000;
RA Wilson H.L., Ou M.S., Aldrich H.C., Maupin-Furlow J.;
RT "Biochemical and physical properties of the Methanococcus jannaschii 20S
RT proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal
RT 26S proteasome.";
RL J. Bacteriol. 182:1680-1692(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT, GATED
RP STRUCTURE, AND SUBUNIT.
RX PubMed=19481527; DOI=10.1016/j.molcel.2009.04.021;
RA Zhang F., Hu M., Tian G., Zhang P., Finley D., Jeffrey P.D., Shi Y.;
RT "Structural insights into the regulatory particle of the proteasome from
RT Methanocaldococcus jannaschii.";
RL Mol. Cell 34:473-484(2009).
CC -!- FUNCTION: Component of the proteasome core, a large protease complex
CC with broad specificity involved in protein degradation. The
CC M.jannaschii proteasome is able to cleave oligopeptides after Glu, Asp,
CC Tyr, Phe, Trp, slightly after Arg, but not after Ala. Thus, displays
CC caspase-like and chymotrypsin-like activities and low level of trypsin-
CC like activity. {ECO:0000255|HAMAP-Rule:MF_02113,
CC ECO:0000269|PubMed:10692374}.
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:10692374};
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, ECO:0000269|PubMed:10692374,
CC ECO:0000269|PubMed:19481527}.
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; L77117; AAB99241.1; -; Genomic_DNA.
DR PIR; D64454; D64454.
DR RefSeq; WP_010870749.1; NC_000909.1.
DR PDB; 3H4P; X-ray; 4.10 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n=7-224.
DR PDBsum; 3H4P; -.
DR AlphaFoldDB; Q58634; -.
DR SMR; Q58634; -.
DR STRING; 243232.MJ_1237; -.
DR MEROPS; T01.002; -.
DR EnsemblBacteria; AAB99241; AAB99241; MJ_1237.
DR GeneID; 1452133; -.
DR KEGG; mja:MJ_1237; -.
DR eggNOG; arCOG00970; Archaea.
DR HOGENOM; CLU_035750_7_2_2; -.
DR InParanoid; Q58634; -.
DR OMA; VDKTGPH; -.
DR OrthoDB; 89767at2157; -.
DR PhylomeDB; Q58634; -.
DR EvolutionaryTrace; Q58634; -.
DR Proteomes; UP000000805; 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; 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; -; 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 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Cytoplasm; Hydrolase; Protease;
KW Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..6
FT /note="Removed in mature form; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
FT /id="PRO_0000026661"
FT CHAIN 7..224
FT /note="Proteasome subunit beta"
FT /id="PRO_0000026662"
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02113"
SQ SEQUENCE 224 AA; 24285 MW; 45B2A0D1EAEF7A58 CRC64;
MDVMKGTTTV GLICDDAVIL ATDKRASLGN LVADKEAKKL YKIDDYIAMT IAGSVGDAQA
IVRLLIAEAK LYKMRTGRNI PPLACATLLS NILHSSRMFP FLTQIIIGGY DLLEGAKLFS
LDPLGGMNEE KTFTATGSGS PIAYGVLEAG YDRDMSVEEG IKLALNALKS AMERDTFSGN
GISLAVITKD GVKIFEDEEI EKILDSMKAK PKKKTTKRSR RKSK
