(data stored in SCRATCH zone)

HOGENOM: PARBH_1_PE1001

ID   PARBH_1_PE1001                       STANDARD;      PRT;   180 AA.
AC   PARBH_1_PE1001; E0TGD6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP-dependent protease subunit HslV; EC=3.4.25 2;
DE   (PARBH_1.PE1001).
GN   Name=hslV; OrderedLocusNames=PB2503_05532;
OS   PARVULARCULA BERMUDENSIS HTCC2503.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Parvularculales;
OC   Parvularculaceae; Parvularcula.
OX   NCBI_TaxID=314260;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PARBH_1.PE1001.
CC       Parvularcula bermudensis HTCC2503 chromosome, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:E0TGD6_PARBH
CC   -!- FUNCTION: Protease subunit of a proteasome-like degradation
CC       complex believed to be a general protein degrading machinery (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-dependent cleavage of peptide bonds with
CC       broad specificity.
CC   -!- ENZYME REGULATION: Allosterically activated by HslU binding (By
CC       similarity).
CC   -!- SUBUNIT: A double ring-shaped homohexamer of HslV is capped on
CC       each side by a ring-shaped HslU homohexamer. The assembly of the
CC       HslU/HslV complex is dependent on binding of ATP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily.
CC   -!- GENE_FAMILY: HOG000064533 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E0TGD6; -.
DR   EMBL; CP002156; ADM09179.1; -; Genomic_DNA.
DR   RefSeq; YP_003854321.1; NC_014414.1.
DR   ProteinModelPortal; E0TGD6; -.
DR   SMR; E0TGD6; 2-177.
DR   GeneID; 9709345; -.
DR   GenomeReviews; CP002156_GR; PB2503_05532.
DR   KEGG; pbr:PB2503_05532; -.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:HAMAP.
DR   GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:InterPro.
DR   HAMAP; MF_00248; HslV; 1; -.
DR   InterPro; IPR022281; ATP-dep_Prtase_HsIV_su.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   Pfam; PF00227; Proteasome; 1.
DR   TIGRFAMs; TIGR03692; ATP_dep_HslV; 1.
DR   HOGENOMDNA; PARBH_1.PE1001; -.
KW   Multispecific proteasome protease;
KW   Allosteric enzyme; Complete proteome; Cytoplasm; Hydrolase;
KW   Metal-binding; Protease; Proteasome; Sodium; Threonine protease.
SQ   SEQUENCE   180 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTTILAVQRG REVAVGGDGQ VTLGERVVSK GDAKKVRRLA DGAVLSGFAG GTADAFTLLE
     RLEGKLEQYR GQLLRSAVEL AKDWRTDRYL RRLEAMLIVA DASQMLMVSG LGDVIEPEKT
     GDVGILAIGS GGSYAQAAAT ALAQNTDLSA REIVEKSLII ASGLDVFTND RLIVETLTSA
//

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