ID   CLPY_BACVZ              Reviewed;         467 AA.
AC   A7Z4N6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=ATP-dependent protease ATPase subunit ClpY;
GN   Name=clpY; Synonyms=hslU; OrderedLocusNames=RBAM_015990;
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: 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; CP000560; ABS73962.1; -; Genomic_DNA.
DR   RefSeq; WP_007409775.1; NC_009725.2.
DR   AlphaFoldDB; A7Z4N6; -.
DR   SMR; A7Z4N6; -.
DR   STRING; 326423.RBAM_015990; -.
DR   EnsemblBacteria; ABS73962; ABS73962; RBAM_015990.
DR   KEGG; bay:RBAM_015990; -.
DR   HOGENOM; CLU_033123_0_0_9; -.
DR   OMA; KYGMIKT; -.
DR   Proteomes; UP000001120; 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.
FT   CHAIN           1..467
FT                   /note="ATP-dependent protease ATPase subunit ClpY"
FT                   /id="PRO_1000012700"
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         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         417
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  52351 MW;  528256A6FE10D9FE CRC64;
     MENKPLTPRQ IVDRLDQYIV GQQDAKKAVA VALRNRYRRS LLDEKLRDEI VPKNILMMGP
     TGVGKTEIAR RIAKLTGAPF IKIEATKFTE VGYVGRDVES MVRDLVETSV RLIKEEKISE
     VKEQAEENAN KRIVRLLVPG KKKQAGVKNP FEMLFGGNQA ANDDEADQQE EASLEEKRKR
     MAHQLALGEL EDHYVSVEVE EQQPSMFDML QGSGMEQMGM NMQDALSNLV PKKKKRRKMT
     VREARKVLTN EEAGKLIDMD EVGQEAVLRA EEGGIIFIDE IDKIAKNGGA SSSADVSREG
     VQRDILPIVE GSTVVTKYGS VKTDHVLFIA AGAFHMAKPS DLIPELQGRF PIRVELSKLT
     VDDFVKILVE PDNALLKQYQ ALLQTEGISL EFSDEAIRKI AEVAYHVNQD TDNIGARRLH
     TILERLLEDL SFEAPDVTME KVAITPQYVE EKLGTIANNK DLSQFIL