ID   HSLU_LACLE              Reviewed;         464 AA.
AC   Q48735;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 103.
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};
OS   Lactobacillus leichmannii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=28039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 4797 / DSM 20076 / BCRC 10699 / JCM 1148 / NBRC 3073 / NCIMB
RC   7854 / 326 / F59;
RX   PubMed=8867465; DOI=10.1007/s002849900042;
RA   Becker J., Brendel M.;
RT   "Molecular characterization of the xerC gene of Lactobacillus leichmannii
RT   encoding a site-specific recombinase and two adjacent heat shock genes.";
RL   Curr. Microbiol. 32:232-236(1996).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA59020.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X84261; CAA59020.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q48735; -.
DR   SMR; Q48735; -.
DR   MEROPS; X20.005; -.
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; PF07724; AAA_2; 2.
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..464
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_0000160513"
FT   BINDING         18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         60..65
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         342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         414
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   464 AA;  51881 MW;  69C6BC9628C1B312 CRC64;
     MREKTPKQIV DLLDKYIVGQ NEAKKSVAIA LYNRYRRAQL PEDVQKDITP KNILMAGPTG
     VGKTEIARRL ADIVDAPFVK VEATKFTEVG YVGRDVESMV RDLANEAVRI VEKEEFVKVE
     GQAIRQANKT LVRLLVPGVK RNNRQNQMQQ MQEMIQSLLA GGGMSEETEE VTDEIRNQRL
     SVAEKLDRGL LENEEVTIEV EQAPKANPMG DMMGQMGMDM SSMLGDMLPK KKVKRTLPVS
     QARKLLVQEE EKKLVNYDDI YQKAMDRAGQ SGIIFIDEID KITAADKRNS AGVSREGVQR
     DILPIVEGST VSTKYGPLST DHILFIAAGA FAESKPSDLI PELQGRFPIR VELDALTKDD
     FVRILKDPQN SLLKQYIALL KADGVDLVFT AEAVDKIAEI AFEVNQGTDN IGARRLATIL
     EKLLEEVLYE GPDMEMGQIT ITQAYVEQKL SDIVKNKDLT KFIL