ID A0A291JKR0_9STAP Unreviewed; 180 AA.
AC A0A291JKR0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ECO:0000313|EMBL:RIO43155.1};
GN ORFNames=BJD96_08395 {ECO:0000313|EMBL:ATH60319.1}, BUZ60_05665
GN {ECO:0000313|EMBL:RIO43155.1}, BUZ61_03405
GN {ECO:0000313|EMBL:PTK60097.1}, CD130_08605
GN {ECO:0000313|EMBL:PNZ97307.1}, NCTC13834_01688
GN {ECO:0000313|EMBL:SUM55325.1};
OS Staphylococcus nepalensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=214473 {ECO:0000313|EMBL:ATH60319.1, ECO:0000313|Proteomes:UP000217956};
RN [1] {ECO:0000313|Proteomes:UP000240400, ECO:0000313|Proteomes:UP000265695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNUC 4025 {ECO:0000313|EMBL:RIO43155.1,
RC ECO:0000313|Proteomes:UP000265695}, and SNUC 4337
RC {ECO:0000313|EMBL:PTK60097.1, ECO:0000313|Proteomes:UP000240400};
RX PubMed=28066335; DOI=.3389/fmicb.2016.01990;
RA Naushad S., Barkema H.W., Luby C., Condas L.A., Nobrega D.B., Carson D.A.,
RA De Buck J.;
RT "Comprehensive Phylogenetic Analysis of Bovine Non-aureus Staphylococci
RT Species Based on Whole-Genome Sequencing.";
RL Front. Microbiol. 7:1990-1990(2016).
RN [2] {ECO:0000313|EMBL:ATH60319.1, ECO:0000313|Proteomes:UP000217956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1 {ECO:0000313|EMBL:ATH60319.1,
RC ECO:0000313|Proteomes:UP000217956};
RA Nam Y.-D., Kang J., Chung W.-H.;
RT "Complete genome sequence of Staphylococcus nepalensis JS1.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:PNZ97307.1, ECO:0000313|Proteomes:UP000236280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15150 {ECO:0000313|EMBL:PNZ97307.1,
RC ECO:0000313|Proteomes:UP000236280};
RA Cole K., Golubchik T., Russell J., Foster D., Llewelyn M., Wilson D.,
RA Crook D., Paul J.;
RT "Draft genome sequences of 64 type strains of genus Staph aureus.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:PTK60097.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SNUC 4337 {ECO:0000313|EMBL:PTK60097.1};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:SUM55325.1, ECO:0000313|Proteomes:UP000254412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13834 {ECO:0000313|EMBL:SUM55325.1,
RC ECO:0000313|Proteomes:UP000254412};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:RIO43155.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SNUC 4025 {ECO:0000313|EMBL:RIO43155.1};
RA Parvin R., Begum J.A., Chowdhury E.H., Islam M.R., Harder T.;
RL Submitted (SEP-2018) 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; CP017460; ATH60319.1; -; Genomic_DNA.
DR EMBL; PPRR01000140; PNZ97307.1; -; Genomic_DNA.
DR EMBL; PZHR01000010; PTK60097.1; -; Genomic_DNA.
DR EMBL; QXVN01000017; RIO43155.1; -; Genomic_DNA.
DR EMBL; UHDS01000001; SUM55325.1; -; Genomic_DNA.
DR KEGG; snl:BJD96_08395; -.
DR OrthoDB; 9804884at2; -.
DR Proteomes; UP000217956; Chromosome.
DR Proteomes; UP000236280; Unassembled WGS sequence.
DR Proteomes; UP000240400; Unassembled WGS sequence.
DR Proteomes; UP000254412; Unassembled WGS sequence.
DR Proteomes; UP000265695; 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|HAMAP-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 Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_00248};
KW Threonine protease {ECO:0000256|HAMAP-Rule:MF_00248}.
FT ACT_SITE 8
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"
FT BINDING 171
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00248"
SQ SEQUENCE 180 AA; 19576 MW; 2F14B6E6BD709C4E CRC64;
MSTSIHATTI FAVQHNGHSA MAGDGQVTLG EQVIMKQTAR KVRRLYNDKV LAGFAGSVAD
AFTLFEKFET KLQQFSGNLE RAAVELAQEW RGDKQLRQLE AMLIVMDKES ILVVSGTGEV
IAPDDDLIAI GSGGNYALSA GRALKRHATD LSAREMAYES LKVASDICVF TNDQIVVEEL
//
