ID A0A240TQ09_9BURK Unreviewed; 187 AA. AC A0A240TQ09; A0A240U081; A0A240UAD7; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 24-JAN-2024, entry version 23. DE RecName: Full=ATP-dependent protease subunit HslV {ECO:0000256|HAMAP-Rule:MF_00248}; DE EC=3.4.25.2 {ECO:0000256|HAMAP-Rule:MF_00248}; GN Name=hslV {ECO:0000256|HAMAP-Rule:MF_00248}; GN ORFNames=CBP33_02980 {ECO:0000313|EMBL:ART47217.1}, CBP34_02925 GN {ECO:0000313|EMBL:ART50834.1}, CBP36_03400 GN {ECO:0000313|EMBL:ART58035.1}; OS Acidovorax carolinensis. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=553814 {ECO:0000313|EMBL:ART47217.1, ECO:0000313|Proteomes:UP000194504}; RN [1] {ECO:0000313|Proteomes:UP000194432, ECO:0000313|Proteomes:UP000194440} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NA2 {ECO:0000313|EMBL:ART47217.1}, NA3 RC {ECO:0000313|EMBL:ART50834.1}, and P4 {ECO:0000313|EMBL:ART58035.1}; RA Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H., Wright F.A., RA Aitken M.D.; RT "Polyphasic characterization of four soil-derived phenanthrene-degrading RT Acidovorax strains and proposal of Acidovorax phenanthrenivorans sp. nov."; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protease subunit of a proteasome-like degradation complex CC believed to be a general protein degrading machinery. CC {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_00248}; CC -!- ACTIVITY REGULATION: Allosterically activated by HslU binding. CC {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_00248}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00248}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily. CC {ECO:0000256|ARBA:ARBA00006053, ECO:0000256|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; CP021359; ART47217.1; -; Genomic_DNA. DR EMBL; CP021361; ART50834.1; -; Genomic_DNA. DR EMBL; CP021366; ART58035.1; -; Genomic_DNA. DR AlphaFoldDB; A0A240TQ09; -. DR KEGG; acid:CBP33_02980; -. DR KEGG; acin:CBP34_02925; -. DR KEGG; acip:CBP36_03400; -. DR KEGG; acis:CBP35_15540; -. DR OrthoDB; 9804884at2; -. DR Proteomes; UP000194432; Chromosome. DR Proteomes; UP000194440; Chromosome. DR Proteomes; UP000194504; 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 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 {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP- KW Rule:MF_00248}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00248}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00248}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00248}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00248}; KW Reference proteome {ECO:0000313|Proteomes:UP000194432}; KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_00248}; KW Threonine protease {ECO:0000256|ARBA:ARBA00022698, ECO:0000256|HAMAP- KW Rule:MF_00248}. FT ACT_SITE 13 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248" FT BINDING 172 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248" FT BINDING 175 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248" FT BINDING 178 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248" SQ SEQUENCE 187 AA; 20089 MW; 788CB9BF02A32558 CRC64; MDQSSQTPVF HGTTILSVRR QTPQGLQVAI GGDGQVTLGN IVVKGTARKV RKLYHGKVLA GFAGATADAF TLFERFEAKL EKHQGHLTRA AIELTKDWRT DRVLRRLEAM LAVADASASL IITGNGDVLE PEQGIVSIGS GGAYAHSAAK ALLNHTDLSA QDIVKRSLEI AGELCIYTNM NHTIETL //