HSLU_ESCF3
ID HSLU_ESCF3 Reviewed; 443 AA.
AC B7LUS3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000255|HAMAP-Rule:MF_00249};
DE AltName: Full=Heat shock protein 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=EFER_3841;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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 -!- INDUCTION: By heat shock. {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; CU928158; CAQ91276.1; -; Genomic_DNA.
DR RefSeq; WP_001293345.1; NC_011740.1.
DR AlphaFoldDB; B7LUS3; -.
DR SMR; B7LUS3; -.
DR EnsemblBacteria; CAQ91276; CAQ91276; EFER_3841.
DR GeneID; 60902750; -.
DR KEGG; efe:EFER_3841; -.
DR HOGENOM; CLU_033123_0_0_6; -.
DR OMA; KYGMIKT; -.
DR OrthoDB; 718259at2; -.
DR BioCyc; EFER585054:EFER_RS19195-MON; -.
DR Proteomes; UP000000745; 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; -; 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; 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; Stress response.
FT CHAIN 1..443
FT /note="ATP-dependent protease ATPase subunit HslU"
FT /id="PRO_1000119107"
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; 49581 MW; D219DEAD26DEAA4C CRC64;
MSEMTPREIV SELDKHIIGQ DNAKRSVAIA LRNRWRRMQL NEELRHEVTP KNILMIGPTG
VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDAAVKM VRVQAIEKNR
YRAEELAEER ILDVLIPPAK NNWGQTEQQQ EPSAARQAFR KKLREGQLDD KEIEIDLAAA
PMGVEIMAPP GMEEMTSQLQ SMFQNLGGQK QKARKLKIKD AMKLLIEEEA AKLVNPEELK
QDAIDAVEQH GIVFIDEIDK ICKRGESSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD
HILFIASGAF QIAKPSDLIP ELQGRLPIRV ELQALTTSDF ERILTEPNAS ITVQYKALMA
TEGVNIEFTE SGIKRIAEAA WQVNESTENI GARRLHTVLE RLMEEISYDA SDLSGQSITI
DADYVSKHLD ALVADEDLSR FIL
