ID HSLV_PHOLL Reviewed; 176 AA. AC Q7MYC2; DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-JUN-2018, entry version 93. DE RecName: Full=ATP-dependent protease subunit HslV {ECO:0000255|HAMAP-Rule:MF_00248}; DE EC=3.4.25.2 {ECO:0000255|HAMAP-Rule:MF_00248}; GN Name=hslV {ECO:0000255|HAMAP-Rule:MF_00248}; GN OrderedLocusNames=plu4762; OS Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP OS 105565 / TT01). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Photorhabdus. OX NCBI_TaxID=243265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15139 / CIP 105565 / TT01; RX PubMed=14528314; DOI=10.1038/nbt886; RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., RA Medigue C., Lanois A., Powell K., Siguier P., Vincent R., Wingate V., RA Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.; RT "The genome sequence of the entomopathogenic bacterium Photorhabdus RT luminescens."; RL Nat. Biotechnol. 21:1307-1313(2003). CC -!- FUNCTION: Protease subunit of a proteasome-like degradation CC complex believed to be a general protein degrading machinery. CC {ECO:0000255|HAMAP-Rule:MF_00248}. CC -!- CATALYTIC ACTIVITY: ATP-dependent cleavage of peptide bonds with CC broad specificity. {ECO:0000255|HAMAP-Rule:MF_00248}. CC -!- ENZYME REGULATION: Allosterically activated by HslU binding. CC {ECO:0000255|HAMAP-Rule:MF_00248}. 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. CC {ECO:0000255|HAMAP-Rule:MF_00248}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00248}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00248}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX571874; CAE17134.1; -; Genomic_DNA. DR RefSeq; WP_011148827.1; NC_005126.1. DR ProteinModelPortal; Q7MYC2; -. DR SMR; Q7MYC2; -. DR STRING; 243265.plu4762; -. DR MEROPS; T01.006; -. DR EnsemblBacteria; CAE17134; CAE17134; plu4762. DR KEGG; plu:plu4762; -. DR eggNOG; ENOG4108R5P; Bacteria. DR eggNOG; COG5405; LUCA. DR HOGENOM; HOG000064533; -. DR KO; K01419; -. DR OMA; IMKGNAR; -. DR OrthoDB; POG091H024X; -. DR BioCyc; PLUM243265:PLU_RS23630-MONOMER; -. DR Proteomes; UP000002514; Chromosome. DR GO; GO:0009376; C:HslUV protease complex; IEA:InterPro. 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 CDD; cd01913; protease_HslV; 1. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_00248; HslV; 1. DR InterPro; IPR022281; ATP-dep_Prtase_HsIV_su. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR PANTHER; PTHR32194; PTHR32194; 1. DR Pfam; PF00227; Proteasome; 1. DR PIRSF; PIRSF039093; HslV; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR03692; ATP_dep_HslV; 1. DR PROSITE; PS51476; PROTEASOME_BETA_2; 1. PE 3: Inferred from homology; KW Allosteric enzyme; Complete proteome; Cytoplasm; Hydrolase; KW Metal-binding; Protease; Reference proteome; Sodium; KW Threonine protease. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 176 ATP-dependent protease subunit HslV. FT /FTId=PRO_0000148130. FT ACT_SITE 2 2 {ECO:0000255|HAMAP-Rule:MF_00248}. FT METAL 157 157 Sodium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00248}. FT METAL 160 160 Sodium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00248}. FT METAL 163 163 Sodium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00248}. SQ SEQUENCE 176 AA; 19082 MW; BF27DB8A8D35C89A CRC64; MTTIVSVRRN GQVVIGGDGQ ATMGNTVMKG NVRKVRRLYN DKVIAGFAGG TADAFTLFEL FERKLEMHQG HLTKAAVELA KDWRTDRMLR KLEALLAVAD ENTSLIITGN GDVIQPENDL IAIGSGGPFA QSAARAMLEN TDLGARQIAE KALTIAGDIC IYTNHNHNFE ELPSKA //