ID   HSLU_BURCM              Reviewed;         447 AA.
AC   Q0BAX8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Bamb_3139;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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}.
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DR   EMBL; CP000440; ABI88695.1; -; Genomic_DNA.
DR   RefSeq; WP_011658199.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BAX8; -.
DR   SMR; Q0BAX8; -.
DR   STRING; 339670.Bamb_3139; -.
DR   EnsemblBacteria; ABI88695; ABI88695; Bamb_3139.
DR   GeneID; 44693797; -.
DR   KEGG; bam:Bamb_3139; -.
DR   PATRIC; fig|339670.21.peg.1720; -.
DR   eggNOG; COG1220; Bacteria.
DR   OMA; KYGMIKT; -.
DR   Proteomes; UP000000662; Chromosome 1.
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; Stress response.
FT   CHAIN           1..447
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_1000012713"
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         259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         325
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         397
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   447 AA;  49761 MW;  376B4C93FDD0BA31 CRC64;
     MSTMTPAEIV SELDKHIIGQ AKAKKAVAVA LRNRWRRQQV GEPLRQEITP KNILMIGPTG
     VGKTEIARRL AKLADAPFVK IEATKFTEVG YVGRDVDSIV RDLIEISVKQ TREAEMRKVR
     TKATDQAEDR ILDVLLPQPR AVGFGGNADH ANDDNNATRQ TFRKRLREGQ LDDKEVELDL
     EQPSAGMDIM APPGMEEMTE QIRSMFSNLG SGKKQRRKVK IKEALKLLTD EEAAKMLNDE
     EVKTKAVQNV EQNGIVFLDE IDKITSRNNE GSGGEVSRQG VQRDLLPLVE GTTVNTKYGM
     VKTDHILFIA SGAFHLAKPS DLIPELQGRF PIRVELDSLS VEDFEAILDA TDASLVKQYQ
     ALLATEDVQL EFAADGIRRL AEIAYAVNEK TENIGARRLY TVIEKLLEEV SFSAGNHAGE
     RVTIDAKYVE HALGEVSQDE DLSRYVL