HSLV_THEMA
ID HSLV_THEMA Reviewed; 176 AA.
AC Q9WYZ1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ATP-dependent protease subunit HslV;
DE EC=3.4.25.2;
DE Flags: Precursor;
GN Name=hslV; OrderedLocusNames=TM_0521;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 6-176 IN COMPLEX WITH SODIUM,
RP FUNCTION, PROPEPTIDE, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12646382; DOI=10.1016/s0301-4622(02)00297-1;
RA Song H.K., Bochtler M., Azim M.K., Hartmann C., Huber R., Ramachandran R.;
RT "Isolation and characterization of the prokaryotic proteasome homolog HslVU
RT (ClpQY) from Thermotoga maritima and the crystal structure of HslV.";
RL Biophys. Chem. 100:437-452(2003).
CC -!- FUNCTION: Protease subunit of a proteasome-like degradation complex
CC believed to be a general protein degrading machinery.
CC {ECO:0000269|PubMed:12646382}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent cleavage of peptide bonds with broad
CC specificity.; EC=3.4.25.2; Evidence={ECO:0000269|PubMed:12646382};
CC -!- ACTIVITY REGULATION: Allosterically activated by HslU binding.
CC {ECO:0000250}.
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:0000269|PubMed:12646382}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: According to PubMed:12646382 the propeptide is
CC autoprocessed in 20% of the cases in the expression system (E.coli).
CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD35606.1; -; Genomic_DNA.
DR PIR; G72365; G72365.
DR RefSeq; NP_228331.1; NC_000853.1.
DR RefSeq; WP_004081403.1; NZ_CP011107.1.
DR PDB; 1M4Y; X-ray; 2.10 A; A/B/C=6-176.
DR PDBsum; 1M4Y; -.
DR AlphaFoldDB; Q9WYZ1; -.
DR SMR; Q9WYZ1; -.
DR STRING; 243274.THEMA_02070; -.
DR MEROPS; T01.006; -.
DR EnsemblBacteria; AAD35606; AAD35606; TM_0521.
DR KEGG; tma:TM0521; -.
DR eggNOG; COG5405; Bacteria.
DR InParanoid; Q9WYZ1; -.
DR OMA; IMKGNAR; -.
DR OrthoDB; 1129370at2; -.
DR EvolutionaryTrace; Q9WYZ1; -.
DR Proteomes; UP000008183; 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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Cytoplasm; Hydrolase; Metal-binding;
KW Protease; Reference proteome; Sodium; Threonine protease.
FT PROPEP 1..5
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000395618"
FT CHAIN 6..176
FT /note="ATP-dependent protease subunit HslV"
FT /id="PRO_0000148154"
FT ACT_SITE 6
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:12646382"
FT BINDING 164
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:12646382"
FT BINDING 167
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:12646382"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:1M4Y"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1M4Y"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1M4Y"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1M4Y"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1M4Y"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1M4Y"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1M4Y"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:1M4Y"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1M4Y"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:1M4Y"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1M4Y"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1M4Y"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1M4Y"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1M4Y"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:1M4Y"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:1M4Y"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1M4Y"
SQ SEQUENCE 176 AA; 18933 MW; ECE369602A0ABD02 CRC64;
MKFHGTTILV VRRNGQTVMG GDGQVTFGST VLKGNARKVR KLGEGKVLAG FAGSVADAMT
LFDRFEAKLR EWGGNLTKAA VELAKDWRTD RVLRRLEALL LVADKENIFI ISGNGEVIQP
DDDAAAIGSG GPYALAAAKA LLRNTDLSAR EIVEKAMTIA GEICIYTNQN IVIEEV
