HSLV_DECAR
ID HSLV_DECAR Reviewed; 178 AA.
AC Q47JL9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Daro_0203;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
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; CP000089; AAZ44962.1; -; Genomic_DNA.
DR RefSeq; WP_011285972.1; NC_007298.1.
DR AlphaFoldDB; Q47JL9; -.
DR SMR; Q47JL9; -.
DR STRING; 159087.Daro_0203; -.
DR MEROPS; T01.006; -.
DR EnsemblBacteria; AAZ44962; AAZ44962; Daro_0203.
DR KEGG; dar:Daro_0203; -.
DR eggNOG; COG5405; Bacteria.
DR HOGENOM; CLU_093872_1_0_4; -.
DR OMA; IMKGNAR; -.
DR OrthoDB; 1129370at2; -.
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_1000012602"
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; 19336 MW; EECC7609354190E9 CRC64;
MEQYHGTTIL SVRRGNSVAM GGDGQVTLGN IVIKATARKV RRLYNGRILA GFAGGTADAF
TLFERFEAKL DKHQGNLLRS AVELAKDWRS DRALRRLEAM LSVADREVSL IITGNGDVLE
PEQGIVAIGS GGSYAQSAAR ALLENTELAP RDIVTKSLEI AGDICIYTNR NFTLEVLE