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Database: UniProt
Entry: A0A317CV88_9GAMM
LinkDB: A0A317CV88_9GAMM
Original site: A0A317CV88_9GAMM 
ID   A0A317CV88_9GAMM        Unreviewed;       177 AA.
AC   A0A317CV88;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
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=DKW60_03690 {ECO:0000313|EMBL:PWR00253.1};
OS   Leucothrix pacifica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Leucothrix.
OX   NCBI_TaxID=1247513 {ECO:0000313|EMBL:PWR00253.1, ECO:0000313|Proteomes:UP000245539};
RN   [1] {ECO:0000313|EMBL:PWR00253.1, ECO:0000313|Proteomes:UP000245539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 18388 {ECO:0000313|EMBL:PWR00253.1,
RC   ECO:0000313|Proteomes:UP000245539};
RA   Choi A., Baek K.;
RT   "Leucothrix arctica sp. nov., isolated from Arctic seawater.";
RL   Submitted (MAY-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWR00253.1}.
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DR   EMBL; QGKM01000005; PWR00253.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317CV88; -.
DR   OrthoDB; 9804884at2; -.
DR   Proteomes; UP000245539; 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:UP000245539};
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;  19152 MW;  7664D4E2FDD84693 CRC64;
     MEQYRGTTIL SVRRDGKVVI GGDGQVSMGN TVMKGNARKV RRLHNNQVIA GFAGGTADAF
     TLFERFEAKL QEYNGNLTRA AIELAKDWRS DRAMRTLEAL LAVADSETSL IITGNGDVIE
     PEDNLIAIGS GGPFAQSAAR ALLDNTELSA REIVEKGLGI AADICIYTNH NRTIEEL
//
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