ID   CLPQ_BACP2              Reviewed;         181 AA.
AC   A8FD79;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=ATP-dependent protease subunit ClpQ;
DE            EC=3.4.21.-;
GN   Name=clpQ; Synonyms=hslV; OrderedLocusNames=BPUM_1513;
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032;
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(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; CP000813; ABV62196.1; -; Genomic_DNA.
DR   RefSeq; WP_003211247.1; NZ_VEIS01000003.1.
DR   AlphaFoldDB; A8FD79; -.
DR   SMR; A8FD79; -.
DR   STRING; 315750.BPUM_1513; -.
DR   MEROPS; T01.007; -.
DR   EnsemblBacteria; ABV62196; ABV62196; BPUM_1513.
DR   GeneID; 61741105; -.
DR   KEGG; bpu:BPUM_1513; -.
DR   eggNOG; COG5405; Bacteria.
DR   HOGENOM; CLU_093872_1_1_9; -.
DR   OMA; IMKGNAR; -.
DR   OrthoDB; 1129370at2; -.
DR   Proteomes; UP000001355; 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; Reference proteome;
KW   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_1000059014"
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;  19404 MW;  54FA988F7BD98DFF CRC64;
     MSSFHATTIF AVQHKGKSAM AGDGQVTFGQ AVVMKHTAKK VRRLFGGKVL AGFAGSVADA
     FTLFEKFETK LEEYGGNLKR AAVELAKEWR SDKMLRQLEA MLIVMNKDSI LLVSGTGEVI
     EPDDGILAIG SGGNYALSAG RALKTHAGDH LTARDIAKAA LETAGEICVY TNDQITLEEL
     E