ID   CLPY_BACP2              Reviewed;         466 AA.
AC   A8FD80;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=ATP-dependent protease ATPase subunit ClpY;
GN   Name=clpY; Synonyms=hslU; OrderedLocusNames=BPUM_1514;
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: ATPase subunit of a proteasome-like degradation complex; this
CC       subunit has chaperone activity. {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 ClpX chaperone family. HslU subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000813; ABV62197.1; -; Genomic_DNA.
DR   RefSeq; WP_012009950.1; NZ_VEIS01000003.1.
DR   AlphaFoldDB; A8FD80; -.
DR   SMR; A8FD80; -.
DR   STRING; 315750.BPUM_1514; -.
DR   EnsemblBacteria; ABV62197; ABV62197; BPUM_1514.
DR   KEGG; bpu:BPUM_1514; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_9; -.
DR   OMA; KYGMIKT; -.
DR   OrthoDB; 718259at2; -.
DR   Proteomes; UP000001355; Chromosome.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00249; HslU; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004491; HslU.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR48102:SF3; PTHR48102:SF3; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00390; hslU; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..466
FT                   /note="ATP-dependent protease ATPase subunit ClpY"
FT                   /id="PRO_1000059021"
FT   REGION          153..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   466 AA;  52415 MW;  EB6EA33C7CB47818 CRC64;
     MEKKPFTPRE IVEKLDQYII GQLDAKKAVA VALRNRYRRS LLHDKLKDEV VPKNILMIGP
     TGVGKTEIAR RIAKISGAPF IKVEATKFTE VGYVGRDVES MVRDLVETAI RIVKEDKMKD
     VQEEAEKQAN KRLVHLLVPG KKKSQSVKNP FEMLFGGSDE DDRDRDQSSE EVELESTRKR
     IAHQLAMGEL EDHYVTIEVE EQQPSMFDML QGSGMEQMGM NMQDALGNLM PKKKKRRKLT
     VREARKALTA EEASKLIDMD EVSQEAVYKA EQQGIIFIDE IDKIAKSGGA SSADVSREGV
     QRDILPIVEG STVMTKYGAV KTDHVLFVAA GAFHMAKPSD LIPELQGRFP IRVELDKLSI
     EDFVKILTEP DNALLKQYKA LLETEGISLE FSDDAIHKIA EVAYHVNQET DNIGARRLHT
     ILEKLLEELS FEAPDITLGT VTITPQYVEE KLGKIANNKD LSQFIL