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HSLV_BURL3
ID   HSLV_BURL3              Reviewed;         178 AA.
AC   Q39BY1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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};
GN   OrderedLocusNames=Bcep18194_A6441;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) 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: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}.
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DR   EMBL; CP000151; ABB10035.1; -; Genomic_DNA.
DR   RefSeq; WP_011353540.1; NZ_CABVQN010000039.1.
DR   AlphaFoldDB; Q39BY1; -.
DR   SMR; Q39BY1; -.
DR   MEROPS; T01.006; -.
DR   EnsemblBacteria; ABB10035; ABB10035; Bcep18194_A6441.
DR   GeneID; 46327676; -.
DR   KEGG; bur:Bcep18194_A6441; -.
DR   PATRIC; fig|482957.22.peg.3472; -.
DR   HOGENOM; CLU_093872_1_0_4; -.
DR   OMA; IMKGNAR; -.
DR   OrthoDB; 1129370at2; -.
DR   Proteomes; UP000002705; 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 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_1000012592"
FT   ACT_SITE        7
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         162
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         165
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         168
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
SQ   SEQUENCE   178 AA;  19245 MW;  1568B1E7858BFBC5 CRC64;
     MEQFHGTTIV SVRRGDKVAL GGDGQVTLGN IVMKGGARKV RRIYNNQVLV GFAGGTADAF
     SLLDRFEAKL EKHQGNLTRA AVELAKDWRT DRMLRRLEAM LITADATTTL VITGNGDVLD
     PEEGICAIGS GGAYAQAAAR ALAENTELSP REIVEKSLEI AGDMCIYTNH NRIIETIE
 
 
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