(data stored in ACNUC7421 zone)

SWISSPROT: PSB_RHOOB

ID   PSB_RHOOB               Reviewed;         294 AA.
AC   C1ASP7;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
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 PrcB {ECO:0000255|HAMAP-Rule:MF_02113};
DE   Flags: Precursor;
GN   Name=prcB {ECO:0000255|HAMAP-Rule:MF_02113};
GN   OrderedLocusNames=ROP_05820;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the proteasome core, a large protease
CC       complex with broad specificity involved in protein degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_02113}.
CC   -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC       specificity. {ECO:0000255|HAMAP-Rule:MF_02113}.
CC   -!- ENZYME REGULATION: The formation of the proteasomal ATPase ARC-20S
CC       proteasome complex, likely via the docking of the C-termini of ARC
CC       into the intersubunit pockets in the alpha-rings, may trigger
CC       opening of the gate for substrate entry. Interconversion between
CC       the open-gate and close-gate conformations leads to a dynamic
CC       regulation of the 20S proteasome proteolysis activity.
CC       {ECO:0000255|HAMAP-Rule:MF_02113}.
CC   -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_02113}.
CC   -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14
CC       beta subunits that assemble into four stacked heptameric rings,
CC       resulting in a barrel-shaped structure. The two inner rings, each
CC       composed of seven catalytic beta subunits, are sandwiched by two
CC       outer rings, each composed of seven alpha subunits. The catalytic
CC       chamber with the active sites is on the inside of the barrel. Has
CC       a gated structure, the ends of the cylinder being occluded by the
CC       N-termini of the alpha-subunits. Is capped by the proteasome-
CC       associated ATPase, ARC. {ECO:0000255|HAMAP-Rule:MF_02113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family.
CC       {ECO:0000255|HAMAP-Rule:MF_02113}.
DR   EMBL; AP011115; BAH48829.1; -; Genomic_DNA.
DR   RefSeq; WP_012687836.1; NC_012522.1.
DR   SMR; C1ASP7; -.
DR   STRING; 632772.ROP_05820; -.
DR   MEROPS; T01.005; -.
DR   EnsemblBacteria; BAH48829; BAH48829; ROP_05820.
DR   KEGG; rop:ROP_05820; -.
DR   PATRIC; fig|632772.20.peg.640; -.
DR   eggNOG; ENOG4105KPK; Bacteria.
DR   eggNOG; COG0638; LUCA.
DR   HOGENOM; HOG000245308; -.
DR   KO; K03433; -.
DR   OMA; TMCAGVT; -.
DR   OrthoDB; POG091H08LD; -.
DR   UniPathway; UPA00997; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_02113_B; Proteasome_B_B; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR022483; Pept_T1A_Psome_suB_actinobac.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR03690; 20S_bact_beta; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1ASP7.
DR   SWISS-2DPAGE; C1ASP7.
KW   Autocatalytic cleavage; Complete proteome; Cytoplasm; Hydrolase;
KW   Protease; Proteasome; Threonine protease; Zymogen.
FT   PROPEP        1     65       Removed in mature form; by autocatalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_02113}.
FT                                /FTId=PRO_0000397566.
FT   CHAIN        66    294       Proteasome subunit beta.
FT                                /FTId=PRO_0000397567.
FT   ACT_SITE     66     66       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_02113}.
SQ   SEQUENCE   294 AA;  31074 MW;  E594198D5A993F7B CRC64;
     MTADRPALRT GDGDTRLSFG SNLSSFTEYL RGHAPELLPE NRIGHRSHST RGGDGMESGD
     LAPHGTTIVA LTYKGGVLLA GDRRATQGNL IASRDVEKVY VTDEYSAAGI AGTAGIAIEL
     VRLFAVELEH YEKIEGVPLT FDGKANRLAS MVRGNLGAAM QGLAVVPLLV GYDLDADEEA
     RAGRIVSYDV VGGRYEERAG YHAVGSGSLF AKSALKKIYS PDSDEETALR AAIESLYDAA
     DDDSATGGPD LTRGIYPTAV TITQAGAVHV SEETTSELAR RIVAERTEEG GSAR
//

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