HSLV_DESAP
ID HSLV_DESAP Reviewed; 177 AA.
AC B1I260;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Daud_0603;
OS Desulforudis audaxviator (strain MP104C).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Candidatus Desulforudis.
OX NCBI_TaxID=477974;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL Submitted (OCT-2007) 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; CP000860; ACA59137.1; -; Genomic_DNA.
DR RefSeq; WP_012301725.1; NC_010424.1.
DR AlphaFoldDB; B1I260; -.
DR SMR; B1I260; -.
DR STRING; 477974.Daud_0603; -.
DR MEROPS; T01.007; -.
DR EnsemblBacteria; ACA59137; ACA59137; Daud_0603.
DR KEGG; dau:Daud_0603; -.
DR eggNOG; COG5405; Bacteria.
DR HOGENOM; CLU_093872_1_0_9; -.
DR OMA; IMKGNAR; -.
DR OrthoDB; 1129370at2; -.
DR Proteomes; UP000008544; Chromosome.
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 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;
KW Reference proteome; Sodium; Threonine protease.
FT CHAIN 1..177
FT /note="ATP-dependent protease subunit HslV"
FT /id="PRO_1000100889"
FT ACT_SITE 6
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 177 AA; 18821 MW; 6C27D83239A8AA9C CRC64;
MTFKGTTIVA VKRDGAVALA GDGQVGLGNG IIVKRDAVKL RRLYKDRVVA GFAGSVADAF
ALFERFEGKL EESQGNLRRA AVQLAKDWRT DKYLRRLEAL LVVADREAVL LISGGGEVIE
PDDGIIAVGS GGAFALAAAR ALARHTALPA VDIAREALQI ASQICVHTND RITVEQV