ID A0A1I6KXP4_9GAMM Unreviewed; 177 AA.
AC A0A1I6KXP4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=ATP-dependent protease subunit HslV {ECO:0000256|HAMAP-Rule:MF_00248};
DE EC=3.4.25.2 {ECO:0000256|HAMAP-Rule:MF_00248};
GN Name=hslV {ECO:0000256|HAMAP-Rule:MF_00248};
GN ORFNames=SAMN05216570_1244 {ECO:0000313|EMBL:SFR95700.1};
OS Dyella sp. OK004.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1855292 {ECO:0000313|EMBL:SFR95700.1, ECO:0000313|Proteomes:UP000198834};
RN [1] {ECO:0000313|EMBL:SFR95700.1, ECO:0000313|Proteomes:UP000198834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK004 {ECO:0000313|EMBL:SFR95700.1,
RC ECO:0000313|Proteomes:UP000198834};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_00248};
CC -!- ACTIVITY REGULATION: Allosterically activated by HslU binding.
CC {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00248}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00248}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily.
CC {ECO:0000256|ARBA:ARBA00006053, ECO:0000256|HAMAP-Rule:MF_00248}.
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DR EMBL; FOZI01000001; SFR95700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6KXP4; -.
DR STRING; 1855292.SAMN05216570_1244; -.
DR OrthoDB; 9804884at2; -.
DR Proteomes; UP000198834; Unassembled WGS sequence.
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; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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 NCBIfam; TIGR03692; ATP_dep_HslV; 1.
DR PANTHER; PTHR32194:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1.
DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PIRSF; PIRSF039093; HslV; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP-
KW Rule:MF_00248};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00248};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00248};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00248};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00248};
KW Reference proteome {ECO:0000313|Proteomes:UP000198834};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_00248};
KW Threonine protease {ECO:0000256|ARBA:ARBA00022698, ECO:0000256|HAMAP-
KW Rule:MF_00248}.
FT ACT_SITE 7
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248"
FT BINDING 162
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248"
FT BINDING 165
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248"
FT BINDING 168
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248"
SQ SEQUENCE 177 AA; 19052 MW; E68A66B1E6F70172 CRC64;
MESFHATTII SVRRNGRVVI GGDGQVTLGN TVMKANARKI RRLGKGDVLA GFAGATADAF
TLFELFEEKL IKHSGNLTRA AVEMAKEWRT DRRLGRLEAM LAVADKDASL LISGNGDVLE
PEHGLIAIGS GGPYAQSAAL ALMENTQMDA REIVEKALKI AGDICIYTNH NTTIEEL
//
