ID   HSLV_SYNWW              Reviewed;         178 AA.
AC   Q0AYP2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Swol_0843;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68162.1; -; Genomic_DNA.
DR   RefSeq; WP_011640267.1; NC_008346.1.
DR   AlphaFoldDB; Q0AYP2; -.
DR   SMR; Q0AYP2; -.
DR   STRING; 335541.Swol_0843; -.
DR   MEROPS; T01.007; -.
DR   EnsemblBacteria; ABI68162; ABI68162; Swol_0843.
DR   KEGG; swo:Swol_0843; -.
DR   eggNOG; COG5405; Bacteria.
DR   HOGENOM; CLU_093872_1_0_9; -.
DR   OMA; IMKGNAR; -.
DR   OrthoDB; 1129370at2; -.
DR   Proteomes; UP000001968; 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;
KW   Reference proteome; Sodium; Threonine protease.
FT   CHAIN           1..178
FT                   /note="ATP-dependent protease subunit HslV"
FT                   /id="PRO_0000336799"
FT   ACT_SITE        5
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   178 AA;  18958 MW;  AD204C64EE9ECF5F CRC64;
     MFQATTIIAV RKGQQTAIAG DGQVTLGQNT IMKQNATKIR RLYEGKVIAG FAGAVADAFT
     LFAKFEEKLK QAGGNLSKAA VEIAREWRSD RILRRLEALL IVADAEKIFI VSGSGELIEP
     DDGIAAIGSG GAYALAAARA LNAFSELNAR EIAVESLKIA SGICVYTNEQ ISVEVIEK