ID   HSLU_AZOSB              Reviewed;         443 AA.
AC   A1K2I6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=azo0424;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL93041.1; -; Genomic_DNA.
DR   RefSeq; WP_011764159.1; NC_008702.1.
DR   AlphaFoldDB; A1K2I6; -.
DR   SMR; A1K2I6; -.
DR   STRING; 62928.azo0424; -.
DR   EnsemblBacteria; CAL93041; CAL93041; azo0424.
DR   KEGG; azo:azo0424; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_4; -.
DR   OMA; KYGMIKT; -.
DR   OrthoDB; 718259at2; -.
DR   Proteomes; UP000002588; 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   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..443
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_1000012699"
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         256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         393
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   443 AA;  49537 MW;  53653AE3D5A2FD7F CRC64;
     MTQMTPPEIV SELDKHIVGQ ARAKKAVAIA LRNRWRRARI DEPLRSEITP KNILMIGPTG
     VGKTEIARRL ARLANAPFIK VEATKFTEVG YVGRDVDTII RDLVEIAIKD GRERAMRVVR
     DRALDAAEDR VLDVLLPPAR PVGFSEPAQP QDSATRQKFR KKLREGELDD KEVEIEVASA
     PMQAEIFAPP GMEELTQQIQ GMFQNLGNSR KKLRKLPIRE ALKLLADEEA ARLINDEEVK
     TEALRAVEQN GIVFLDEVDK IAARADAHGA DVSRQGVQRD LLPLVEGTTI STKYGMIKTD
     HILFIASGAF HLSKPSDLIP ELQGRFPIRV ELESLSVEDF ERILTSTDAC LTRQYEALLA
     TDGVTLSFTP EGIRRLAEIA YQVNEKTENI GARRLYTVME KLLEEVSFEA GKVGVDKLTV
     DAAYVDARLE VLAQREDLAR YVL