ID A0A240TQ09_9BURK Unreviewed; 187 AA. AC A0A240TQ09; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 20-DEC-2017, entry version 3. DE RecName: Full=ATP-dependent protease subunit HslV {ECO:0000256|HAMAP-Rule:MF_00248, ECO:0000256|SAAS:SAAS00347004}; DE EC=3.4.25.2 {ECO:0000256|HAMAP-Rule:MF_00248, ECO:0000256|SAAS:SAAS00347012}; GN Name=hslV {ECO:0000256|HAMAP-Rule:MF_00248}; GN ORFNames=CBP33_02980 {ECO:0000313|EMBL:ART47217.1}; OS Acidovorax sp. NA2. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=1662456 {ECO:0000313|EMBL:ART47217.1, ECO:0000313|Proteomes:UP000194504}; RN [1] {ECO:0000313|EMBL:ART47217.1, ECO:0000313|Proteomes:UP000194504} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NA2 {ECO:0000313|EMBL:ART47217.1}; RA Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H., RA Wright F.A., Aitken M.D.; RT "Polyphasic characterization of four soil-derived phenanthrene- RT degrading Acidovorax strains and proposal of Acidovorax RT phenanthrenivorans sp. nov."; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protease subunit of a proteasome-like degradation CC complex believed to be a general protein degrading machinery. CC {ECO:0000256|HAMAP-Rule:MF_00248, ECO:0000256|SAAS:SAAS00347025}. CC -!- CATALYTIC ACTIVITY: ATP-dependent cleavage of peptide bonds with CC broad specificity. {ECO:0000256|HAMAP-Rule:MF_00248, CC ECO:0000256|SAAS:SAAS00019531}. CC -!- ENZYME 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 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:0000256|HAMAP-Rule:MF_00248, ECO:0000256|SAAS:SAAS00347079}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00248, CC ECO:0000256|SAAS:SAAS00347051}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00248, ECO:0000256|SAAS:SAAS00542229}. 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 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 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 {ECO:0000256|HAMAP-Rule:MF_00248}; KW Complete proteome {ECO:0000313|Proteomes:UP000194504}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00248, KW ECO:0000256|SAAS:SAAS00019484}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00248, KW ECO:0000256|SAAS:SAAS00019520}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00248, KW ECO:0000256|SAAS:SAAS00425254}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00248, KW ECO:0000256|SAAS:SAAS00019529}; KW Sodium {ECO:0000256|HAMAP-Rule:MF_00248, KW ECO:0000256|SAAS:SAAS00019537}; KW Threonine protease {ECO:0000256|HAMAP-Rule:MF_00248, KW ECO:0000256|SAAS:SAAS00019514}. FT ACT_SITE 13 13 {ECO:0000256|HAMAP-Rule:MF_00248}. FT METAL 172 172 Sodium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00248}. FT METAL 175 175 Sodium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00248}. FT METAL 178 178 Sodium; via carbonyl oxygen. FT {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 //