ID   PSB6_TOBAC              Reviewed;         234 AA.
AC   P93395;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Proteasome subunit beta type-6;
DE            EC=3.4.25.1;
DE   AltName: Full=Proteasome delta chain;
DE   AltName: Full=Tobacco cryptogein-induced protein 7;
DE            Short=tcI 7;
DE   Flags: Precursor;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Xanthi;
RX   PubMed=9349250; DOI=10.1023/a:1005833216479;
RA   Petitot A.S., Blein J.P., Pugin A., Suty L.;
RT   "Cloning of two plant cDNAs encoding a beta-type proteasome subunit and a
RT   transformer-2-like SR-related protein: early induction of the corresponding
RT   genes in tobacco cells treated with cryptogein.";
RL   Plant Mol. Biol. 35:261-269(1997).
RN   [2]
RP   REGULATION.
RX   PubMed=10682830; DOI=10.1016/s0014-5793(00)01084-x;
RA   Etienne P., Petitot A.S., Houot V., Blein J.P., Suty L.;
RT   "Induction of tcI 7, a gene encoding a beta-subunit of proteasome, in
RT   tobacco plants treated with elicitins, salicylic acid or hydrogen
RT   peroxide.";
RL   FEBS Lett. 466:213-218(2000).
CC   -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC       is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC       Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC       pH. The proteasome has an ATP-dependent proteolytic activity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1;
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is composed of 28
CC       subunits that are arranged in four stacked rings, resulting in a
CC       barrel-shaped structure. The two end rings are each formed by seven
CC       alpha subunits, and the two central rings are each formed by seven beta
CC       subunits. The catalytic chamber with the active sites is on the inside
CC       of the barrel (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC       Nucleus {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by elicitins (cryptogein and parasiticein),
CC       salicylic acid (SA) and hydrogen peroxide.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; Y09505; CAA70699.1; -; mRNA.
DR   PIR; T03985; T03985.
DR   RefSeq; NP_001312872.1; NM_001325943.1.
DR   AlphaFoldDB; P93395; -.
DR   SMR; P93395; -.
DR   STRING; 4097.P93395; -.
DR   MEROPS; T01.010; -.
DR   PRIDE; P93395; -.
DR   GeneID; 107815086; -.
DR   KEGG; nta:107815086; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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-KW.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
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   PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW   Threonine protease; Zymogen.
FT   PROPEP          1..13
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026639"
FT   CHAIN           14..234
FT                   /note="Proteasome subunit beta type-6"
FT                   /id="PRO_0000026640"
FT   ACT_SITE        14
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   234 AA;  25183 MW;  B18098EF4B8C3EDC CRC64;
     MENTDVDQPH SMGTTIIGVT YNGGVVLGAD SRTSTGMYVA NRASDKITQL TDNVYVCRSG
     SAADSQIVSD YVRYFLHQHT IQLGQPATVK VAANLTRLLS YNNKDRLQTG MIIGGWDKYE
     GGKIYGIPPG GTVLEQPFAI GGSGSSYLYG FFDQAWKEGM TQEEAEKLVV TAVSLAIARD
     GASGGVVRTV TINKDGATRK FYSGDSLQLW HEELEPVNSL LDVVFASSPV PMVS