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Database: UniProt
Entry: W4MAJ1_9BACT
LinkDB: W4MAJ1_9BACT
Original site: W4MAJ1_9BACT 
ID   W4MAJ1_9BACT            Unreviewed;       264 AA.
AC   W4MAJ1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Proteasome subunit beta {ECO:0000313|EMBL:ETX06657.1};
GN   ORFNames=ETSY2_15820 {ECO:0000313|EMBL:ETX06657.1};
OS   Candidatus Entotheonella gemina.
OC   Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia;
OC   Entotheonella.
OX   NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETX06657.1, ECO:0000313|Proteomes:UP000019140};
RN   [1] {ECO:0000313|EMBL:ETX06657.1, ECO:0000313|Proteomes:UP000019140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140};
RX   PubMed=24476823; DOI=10.1038/nature12959;
RA   Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K.,
RA   Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., Helfrich E.J.,
RA   Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., Crusemann M.,
RA   Hentschel U., Abe I., Matsunaga S., Kalinowski J., Takeyama H., Piel J.;
RT   "An environmental bacterial taxon with a large and distinct metabolic
RT   repertoire.";
RL   Nature 506:58-62(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETX06657.1}.
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DR   EMBL; AZHX01000642; ETX06657.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4MAJ1; -.
DR   MEROPS; T01.005; -.
DR   PATRIC; fig|1429439.4.peg.2690; -.
DR   HOGENOM; CLU_035750_2_0_7; -.
DR   Proteomes; UP000019140; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR   CDD; cd01906; proteasome_protease_HslV; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   InterPro; IPR022483; PSB_actinobac.
DR   NCBIfam; TIGR03690; 20S_bact_beta; 1.
DR   PANTHER; PTHR32194:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1.
DR   PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Proteasome {ECO:0000313|EMBL:ETX06657.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019140}.
SQ   SEQUENCE   264 AA;  28914 MW;  DEC267F4824EA202 CRC64;
     MLIQGSYDGS SFFDLLRHDY THLLPLQHLP QLSPGVADLS ATVPFGTTVL ALRFADGIVI
     GGDRQATEGF EVSSRRIEKV YNADDYSVIA IAGAAGPCLE MVKLFQIEME HYQKIEGEVL
     ILEGKANKLA QMIRQNLPAA FQGLIVIPIF AGYDLNTQEG RIYKYDVTGG RYGERDFYST
     GSGSREARST LKKRFEPNLC RDAAVRLALE ALVDAADLDV GTSGPDIHRG IYPVMKIVTK
     NGIEDVGEDE LRPMSEALLA SLKG
//
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