ID   HSLU_HAEDU              Reviewed;         440 AA.
AC   Q7VKB3;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 104.
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}; OrderedLocusNames=HD_2007;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP96719.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017143; AAP96719.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041603593.1; NC_002940.2.
DR   AlphaFoldDB; Q7VKB3; -.
DR   SMR; Q7VKB3; -.
DR   STRING; 233412.HD_2007; -.
DR   EnsemblBacteria; AAP96719; AAP96719; HD_2007.
DR   KEGG; hdu:HD_2007; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_6; -.
DR   Proteomes; UP000001022; 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..440
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_0000160507"
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         59..64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         318
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         390
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   440 AA;  49443 MW;  040A813CC60B3FE8 CRC64;
     MSITPREIVS ELDAHIIGQT EAKRAVAIAL RNRWRRMQLS EDLRQEVTPK NILMIGPTGV
     GKTEIARRLA KLAQAPFIKV EATKFTEVGY VGKEVDSIIK DLTEVSMKLV KEQAVEKNRI
     RAQDAAEDRI LDVLLPPAKD QWGNVQETDN ASTRQIFRKK LREGSLDDKE IDIDVASQVN
     VEIMTPPGME EMTSQLQSLF EGMSPNKTQK RKMKIKDALK VMLDEEAAKL VNQEELKQQA
     IEAVEQHGIV FIDEIDKICK KSGNSGGDVS REGVQRDLLP IIEGSTVNTK YGMVKTDHIL
     FICSGAFQIA RPSDLLPELQ GRLPIHVELK SLTKADFERI LTEPNASLTL QYRELMKTEG
     VTIEFTQDGI SKIAESAFRV NEKTENIGAR RLHTVLERLM DGISFDANER AGEHIVIDEK
     YVATALNDVV ENEDLSRFIL