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 27-NOV-2024, entry version 117. 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}; OrderedLocusNames=plu4762; OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / OS TT01) (Photorhabdus luminescens subsp. laumondii). OC Bacteria; Pseudomonadota; 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., Medigue C., RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M., RA 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 complex CC believed to be a general protein degrading machinery. CC {ECO:0000255|HAMAP-Rule:MF_00248}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-dependent cleavage of peptide bonds with broad CC specificity.; EC=3.4.25.2; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00248}; CC -!- ACTIVITY 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 each CC side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV CC complex is dependent on binding of ATP. {ECO:0000255|HAMAP- CC 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 AlphaFoldDB; Q7MYC2; -. DR SMR; Q7MYC2; -. DR STRING; 243265.plu4762; -. DR MEROPS; T01.006; -. DR GeneID; 24170626; -. DR KEGG; plu:plu4762; -. DR eggNOG; COG5405; Bacteria. DR HOGENOM; CLU_093872_1_0_6; -. DR OrthoDB; 9804884at2; -. DR Proteomes; UP000002514; Chromosome. DR GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-UniRule. 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 protein catabolic process; IEA:InterPro. DR CDD; cd01913; protease_HslV; 1. DR FunFam; 3.60.20.10:FF:000002; ATP-dependent protease subunit HslV; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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 NCBIfam; TIGR03692; ATP_dep_HslV; 1. DR PANTHER; PTHR32194:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1. DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1. DR Pfam; PF00227; Proteasome; 1. DR PIRSF; PIRSF039093; HslV; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR PROSITE; PS51476; PROTEASOME_BETA_2; 1. PE 3: Inferred from homology; KW Allosteric enzyme; Cytoplasm; Hydrolase; Metal-binding; Protease; KW Reference proteome; Sodium; Threonine protease. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..176 FT /note="ATP-dependent protease subunit HslV" FT /id="PRO_0000148130" FT ACT_SITE 2 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248" FT BINDING 157 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248" FT BINDING 160 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248" FT BINDING 163 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="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 //