ID   HSLU_BUCSC              Reviewed;          72 AA.
AC   O69227;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=ATP-dependent protease ATPase subunit HslU;
DE   AltName: Full=Unfoldase HslU;
DE   Flags: Fragment;
GN   Name=hslU;
OS   Buchnera aphidicola subsp. Schlechtendalia chinensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7742976; DOI=10.1111/j.1365-2583.1995.tb00007.x;
RA   Lai C.-Y., Baumann P., Moran N.A.;
RT   "Genetics of the tryptophan biosynthetic pathway of the prokaryotic
RT   endosymbiont (Buchnera) of the aphid Schlechtendalia chinensis.";
RL   Insect Mol. Biol. 4:47-59(1995).
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 (By similarity). {ECO:0000250}.
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 (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; U09184; AAC31219.1; -; Genomic_DNA.
DR   AlphaFoldDB; O69227; -.
DR   SMR; O69227; -.
DR   STRING; 118110.XW81_02690; -.
DR   GO; GO:0009376; C:HslUV protease complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   InterPro; IPR004491; HslU.
DR   PANTHER; PTHR48102:SF3; PTHR48102:SF3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding.
FT   CHAIN           <1..72
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_0000160489"
FT   BINDING         21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   72 AA;  8502 MW;  534077998EAC062A CRC64;
     MRHIAEAAWK VNESIENIGA RRLYTVLEHL MEDISYNSCN NKNELVINID EEYVSKHLDE
     LILNNDLNRF IL