ID HSLV_BURMA Reviewed; 178 AA. AC Q62EZ9; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 07-APR-2021, entry version 89. 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=BMA3254; OS Burkholderia mallei (strain ATCC 23344). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=243160; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23344; RX PubMed=15377793; DOI=10.1073/pnas.0403306101; RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E., RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C., RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S., RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y., RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C., RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.; RT "Structural flexibility in the Burkholderia mallei genome."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004). 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; CP000010; AAU48469.1; -; Genomic_DNA. DR RefSeq; WP_004203414.1; NC_006348.1. DR RefSeq; YP_104728.1; NC_006348.1. DR SMR; Q62EZ9; -. DR STRING; 243160.BMA3254; -. DR MEROPS; T01.006; -. DR EnsemblBacteria; AAU48469; AAU48469; BMA3254. DR GeneID; 56594449; -. DR KEGG; bma:BMA3254; -. DR PATRIC; fig|243160.12.peg.3335; -. DR eggNOG; COG5405; Bacteria. DR HOGENOM; CLU_093872_1_0_4; -. DR OMA; IMKGNAR; -. DR BioCyc; BMAL243160:G1G3W-10235-MONOMER; -. DR Proteomes; UP000006693; Chromosome 1. 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; Cytoplasm; Hydrolase; Metal-binding; Protease; Sodium; KW Threonine protease. FT CHAIN 1..178 FT /note="ATP-dependent protease subunit HslV" FT /id="PRO_0000148097" FT ACT_SITE 7 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248" FT METAL 162 FT /note="Sodium; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248" FT METAL 165 FT /note="Sodium; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248" FT METAL 168 FT /note="Sodium; via carbonyl oxygen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00248" SQ SEQUENCE 178 AA; 19053 MW; 45A55775B1B09B7A CRC64; MEQFHGTTIL SVRRGDKVAL GGDGQVTLGN IVMKGGARKV RRIYNNQVLV GFAGGTADAF SLLDRFEAKL EKHQGNLTRA AVELAKDWRT DRLLRRLEAM LIAADATTTL VITGNGDVLD PEGGICAIGS GGSYAQAAAR ALAENTDLSP REIVEKALGI AGDMCIYTNH NRIIETIE //