ID   HSLU_BORBU              Reviewed;         448 AA.
AC   Q44772; Q57063;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=BB_0295;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RA   Dunn J.J., Butler-Loffredo L., Kieleczawa J., Medalle J., Luft B.J.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=212;
RA   Ge Y., Old I.G., Saint-Girons I., Charon N.W.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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; U43739; AAA85618.1; -; Genomic_DNA.
DR   EMBL; X96685; CAA65468.1; -; Genomic_DNA.
DR   EMBL; L76303; AAB51406.1; -; Genomic_DNA.
DR   EMBL; AE000783; AAC66653.2; -; Genomic_DNA.
DR   PIR; G70136; G70136.
DR   RefSeq; NP_212429.2; NC_001318.1.
DR   RefSeq; WP_002656077.1; NC_001318.1.
DR   AlphaFoldDB; Q44772; -.
DR   SMR; Q44772; -.
DR   STRING; 224326.BB_0295; -.
DR   PRIDE; Q44772; -.
DR   EnsemblBacteria; AAC66653; AAC66653; BB_0295.
DR   KEGG; bbu:BB_0295; -.
DR   PATRIC; fig|224326.49.peg.694; -.
DR   HOGENOM; CLU_033123_0_0_12; -.
DR   OMA; KYGMIKT; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
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; -; 1.
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   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..448
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_0000160480"
FT   BINDING         23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         65..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         263
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         327
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         399
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   CONFLICT        110
FT                   /note="S -> G (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="A -> R (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="D -> E (in Ref. 2; CAA65468/AAB51406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130..131
FT                   /note="VR -> IK (in Ref. 2; CAA65468/AAB51406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="D -> E (in Ref. 2; CAA65468/AAB51406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145
FT                   /note="S -> D (in Ref. 2; CAA65468/AAB51406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="M -> I (in Ref. 2; CAA65468/AAB51406)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   448 AA;  50981 MW;  9A86B1E2ECC3FC03 CRC64;
     MNKLEEHYIV PKDVVAELDK YIIGQDEAKK LVSIALVNRY IRSRLPKEIK DEVMPKNIIM
     IGSTGIGKTE IARRLSKLIK APFIKVEATK YTEVGYVGRD VESMVRDLMS IAVNMVKEEM
     YSTVRDDALV RTEERIVDSL FKGSSNSENM DPNEIKAEEK VKEKLRKKLR AGELDDTTIE
     IQISSKMPFS TIEIFTGGNF EEIDMGIGGL LGNIFDRKKK RELKIKKAKE IILAEELEKL
     VDHENISDIA KSKVENMGII FIDEIDKIAA KNRSGNDVSR EGVQRDILPI IEGSKVNTKY
     GIVDTSHILF IAAGAFNLAK PSDLIPELQG RFPIKVELKS LSIDDLKKIL KQTKNSLIKQ
     YVAMFKVYDL DLKFSEEAID RIAELTFNMN LESENLGARR LHGVMEIVLA DLFFEVPGSK
     LKKFEINLDY VNKKIQINEQ KDLNYYII