ID A0AA91TY86_WOLPI Unreviewed; 184 AA. AC A0AA91TY86; DT 27-MAR-2024, integrated into UniProtKB/TrEMBL. DT 27-MAR-2024, sequence version 1. DT 24-JUL-2024, entry version 3. 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=BTO27_00845 {ECO:0000313|EMBL:PBQ29210.1}; OS Wolbachia pipientis wAus. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=2049495 {ECO:0000313|EMBL:PBQ29210.1, ECO:0000313|Proteomes:UP000218032}; RN [1] {ECO:0000313|EMBL:PBQ29210.1, ECO:0000313|Proteomes:UP000218032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=wAus {ECO:0000313|Proteomes:UP000218032}; RA Ward C.M., Baxter S.W.; RT "Wolbachia endosymbiont of Plutella Australiana."; RL Submitted (DEC-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PBQ29210.1}. 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; MRWX01000004; PBQ29210.1; -; Genomic_DNA. DR RefSeq; WP_052264715.1; NZ_MRWX01000004.1. DR Proteomes; UP000218032; Unassembled WGS sequence. 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:SF7; 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}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00248}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00248}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00248}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00248}; 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 12 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248" FT BINDING 167 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248" FT BINDING 170 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248" FT BINDING 173 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248" SQ SEQUENCE 184 AA; 19856 MW; 0AE705E3628F611D CRC64; MIHHDSSKMY GTTILSIRRD KNVVVIGDGQ VSLGHTVIKS GAKKVRRLSG DSVIAGFAGA TADAFTLFER LESKLDKHPG QLMRACVELA KDWRMDKYLR KLEAMMIVAD KSISLVITGT GDVLEPEDGI AAIGSGGNFA LSAAKALIDV EGVSIEEIAK KAMKIAADIC VYTNHNLIIE KIEE //