ID   HSLV_THEP1              Reviewed;         176 AA.
AC   A5IJQ3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Tpet_0400;
OS   Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS   RKU-1).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-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; CP000702; ABQ46426.1; -; Genomic_DNA.
DR   RefSeq; WP_011943053.1; NC_009486.1.
DR   AlphaFoldDB; A5IJQ3; -.
DR   SMR; A5IJQ3; -.
DR   STRING; 390874.Tpet_0400; -.
DR   MEROPS; T01.006; -.
DR   EnsemblBacteria; ABQ46426; ABQ46426; Tpet_0400.
DR   KEGG; tpt:Tpet_0400; -.
DR   eggNOG; COG5405; Bacteria.
DR   HOGENOM; CLU_093872_1_0_0; -.
DR   OMA; IMKGNAR; -.
DR   Proteomes; UP000006558; 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   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..176
FT                   /note="ATP-dependent protease subunit HslV"
FT                   /id="PRO_0000336802"
FT   ACT_SITE        6
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         161
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         164
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
FT   BINDING         167
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00248"
SQ   SEQUENCE   176 AA;  18963 MW;  ECE37BD7DA0ABD02 CRC64;
     MKFHGTTILV VRRNGQTVMG GDGQVTFGST VLKGNARKVR KLGEGKVLAG FAGSVADAMT
     LFDRFEAKLR EWGGNLTKAA VELAKDWRTD RVLRRLEALL LVADKENIFI ISGNGEVIQP
     DDDAAAIGSG GPYALAAAKA LLRNTDLSAR EIVEKAMMIA GEICIYTNQN IVIEEV