ID   HSLU_BACC4              Reviewed;         463 AA.
AC   B7HDV2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000255|HAMAP-Rule:MF_00249};
DE   AltName: Full=Unfoldase HslU {ECO:0000255|HAMAP-Rule:MF_00249};
GN   Name=hslU {ECO:0000255|HAMAP-Rule:MF_00249};
GN   OrderedLocusNames=BCB4264_A3927;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATPase subunit of a proteasome-like degradation complex; this
CC       subunit has chaperone activity. The binding of ATP and its subsequent
CC       hydrolysis by HslU are essential for unfolding of protein substrates
CC       subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of
CC       its protein substrates and unfolds these before they are guided to HslV
CC       for hydrolysis. {ECO:0000255|HAMAP-Rule:MF_00249}.
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_00249}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00249}.
CC   -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00249}.
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DR   EMBL; CP001176; ACK62492.1; -; Genomic_DNA.
DR   RefSeq; WP_000550078.1; NZ_VEHB01000002.1.
DR   AlphaFoldDB; B7HDV2; -.
DR   SMR; B7HDV2; -.
DR   EnsemblBacteria; ACK62492; ACK62492; BCB4264_A3927.
DR   GeneID; 67508463; -.
DR   KEGG; bcb:BCB4264_A3927; -.
DR   HOGENOM; CLU_033123_0_0_9; -.
DR   OMA; KYGMIKT; -.
DR   Proteomes; UP000007096; 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..463
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_1000189693"
FT   BINDING         19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         61..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   463 AA;  52211 MW;  330162B38A69BF3F CRC64;
     MHLHFTPRQI VEKLDQYIIG QKDAKKAVAV ALRNRYRRSK LAENLRDEIA PKNILMIGPT
     GVGKTEVARR MAKLVGAPFI KVEATKFTEV GYVGRDVESM VRDLVETSVR IVKEEMVVKV
     QDKAEEQANQ RLVEILVPSP EKQSGFKNPL EMLFGGAQNS NQTSDTQEDV EIEKKRQDVE
     RKLAAGLLEE EIVSIEVTEQ QSSMFDMLQG TGMEQMGMNF QDALGSFMPK KTKKRKLSVK
     EARKLLTNEE AQRLIDMDEV TQEAVYRAEQ LGIIFIDEID KIAGKQSNSV DVSREGVQRD
     ILPIVEGSNV ATKYGSVKTD YILFVAAGAF HMSKPSDLIP ELQGRFPIRV ELTKLSTDDF
     VKILIEPDNA LIKQYMALLA TEGIEIEFSD EAIRKIAEIA YQVNQDTDNI GARRLHTIME
     KLLEDLSFEA SEITLEKITI TPQYVEEKLA TIAKNKDVSQ FIL