ID   HSLU_STAAT              Reviewed;         467 AA.
AC   A8Z3T4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=USA300HOU_1185;
OS   Staphylococcus aureus (strain USA300 / TCH1516).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=451516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300 / TCH1516;
RX   PubMed=17986343; DOI=10.1186/1471-2180-7-99;
RA   Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S.,
RA   Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O.,
RA   Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M.,
RA   Hemphill L., Ding Y., Dugan S., Blyth P.R., Buhay C.J., Dinh H.H.,
RA   Hawes A.C., Holder M., Kovar C.L., Lee S.L., Liu W., Nazareth L.V.,
RA   Wang Q., Zhou J., Kaplan S.L., Weinstock G.M.;
RT   "Subtle genetic changes enhance virulence of methicillin resistant and
RT   sensitive Staphylococcus aureus.";
RL   BMC Microbiol. 7:99-99(2007).
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; CP000730; ABX29200.1; -; Genomic_DNA.
DR   RefSeq; WP_000379054.1; NC_010079.1.
DR   AlphaFoldDB; A8Z3T4; -.
DR   SMR; A8Z3T4; -.
DR   KEGG; sax:USA300HOU_1185; -.
DR   HOGENOM; CLU_033123_0_0_9; -.
DR   OMA; KYGMIKT; -.
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 HslU"
FT                   /id="PRO_1000078460"
FT   REGION          149..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         64..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         280
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         417
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   467 AA;  52315 MW;  3FC0E37C09E74891 CRC64;
     MDTAGIRLTP KEIVSKLNEY IVGQNDAKRK VAIALRNRYR RSLLDEESKQ EISPKNILMI
     GPTGVGKTEI ARRMAKVVGA PFIKVEATKF TEVGYVGRDV ESMVRDLVDV SVRLVKAQKK
     SLVQDEATAK ANEKLVKLLV PSMKKKASQT NNPLESLFGG AIPNFGQNNE DEEEPPTEEI
     KTKRSEIKRQ LEEGKLEKEK VRIKVEQDPG ALGMLGTNQN QQMQEMMNQL MPKKKVEREV
     AVETARKILA DSYADELIDQ ESANQEALEL AEQMGIIFID EIDKVATNNH NSGQDVSRQG
     VQRDILPILE GSVIQTKYGT VNTEHMLFIG AGAFHVSKPS DLIPELQGRF PIRVELDSLS
     VEDFVRILTE PKLSLIKQYE ALLQTEEVTV NFTDEAITRL AEIAYQVNQD TDNIGARRLH
     TILEKMLEDL SFEAPSMPNA VVDITPQYVD DKLKSISTNK DLSAFIL