HSLV_PARPJ
ID HSLV_PARPJ Reviewed; 178 AA.
AC B2T1N9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Bphyt_0343;
OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS (Burkholderia phytofirmans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=398527;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX PubMed=21551308; DOI=10.1128/jb.05055-11;
RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT "Complete genome sequence of the plant growth-promoting endophyte
RT Burkholderia phytofirmans strain PsJN.";
RL J. Bacteriol. 193:3383-3384(2011).
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; CP001052; ACD14768.1; -; Genomic_DNA.
DR RefSeq; WP_012431411.1; NC_010681.1.
DR AlphaFoldDB; B2T1N9; -.
DR SMR; B2T1N9; -.
DR STRING; 398527.Bphyt_0343; -.
DR MEROPS; T01.006; -.
DR EnsemblBacteria; ACD14768; ACD14768; Bphyt_0343.
DR KEGG; bpy:Bphyt_0343; -.
DR eggNOG; COG5405; Bacteria.
DR HOGENOM; CLU_093872_1_0_4; -.
DR OMA; IMKGNAR; -.
DR OrthoDB; 1129370at2; -.
DR Proteomes; UP000001739; 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_1000100882"
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; 19027 MW; B90A5269C8AB6D31 CRC64;
MEQFHGTTIV SVRRGDKVAL GGDGQVTLGN IVMKGGAKKV RRIYNGKVLV GFAGGTADAF
SLLDRFEAKL EKHQGNLTRA AVELAKDWRT DRMLRRLEAM LITADATTTL VITGNGDVLD
PEGGICAIGS GGAYAQAAAT ALAHNTELSP REIVEKSLEI AGDMCIYTNH NRVIETIE