ID   CLPQ_BACVZ              Reviewed;         181 AA.
AC   A7Z4N5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=ATP-dependent protease subunit ClpQ;
DE            EC=3.4.21.-;
GN   Name=clpQ; Synonyms=hslV; OrderedLocusNames=RBAM_015980;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
CC   -!- FUNCTION: Protease subunit of a proteasome-like degradation complex.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: A double ring-shaped homohexamer of ClpQ is capped on each
CC       side by a ring-shaped ClpY homohexamer. The assembly of the ClpQ/ClpY
CC       complex is dependent on binding of ATP (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000560; ABS73961.1; -; Genomic_DNA.
DR   RefSeq; WP_003154267.1; NC_009725.2.
DR   AlphaFoldDB; A7Z4N5; -.
DR   SMR; A7Z4N5; -.
DR   STRING; 326423.RBAM_015980; -.
DR   MEROPS; T01.007; -.
DR   EnsemblBacteria; ABS73961; ABS73961; RBAM_015980.
DR   GeneID; 66326396; -.
DR   KEGG; bay:RBAM_015980; -.
DR   HOGENOM; CLU_093872_1_1_9; -.
DR   OMA; IMKGNAR; -.
DR   Proteomes; UP000001120; 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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
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   Cytoplasm; Hydrolase; Metal-binding; Protease; Serine protease; Sodium.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..181
FT                   /note="ATP-dependent protease subunit ClpQ"
FT                   /id="PRO_1000012577"
FT   ACT_SITE        2
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   181 AA;  19489 MW;  A229130709EB147B CRC64;
     MSSFHATTIF AVQHNGKSAM SGDGQVTFGQ AVVMKHTARK VRKLFNGKVL AGFAGSVADA
     FTLFEMFEAK LEEYNGNLKR ASVELAKEWR SDKVLRKLEA MLIVMNQDTL LLVSGTGEVI
     EPDDGILAIG SGGNYALSAG RALKTYAGEN LSAKDIAKAA LKIAGEICVY TNDQIILEEL
     E