HSLU_BUCAP
ID HSLU_BUCAP Reviewed; 443 AA.
AC Q9Z617;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 126.
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=BUsg_558;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-443.
RA Clark M.A., Baumann P., Moran M.A.;
RT "Buchnera plasmid-associated trpEG probably originated from a chromosomal
RT location between hslU and fpr.";
RL Submitted (NOV-1998) 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; AE013218; AAM68096.1; -; Genomic_DNA.
DR EMBL; AF108665; AAD19633.1; -; Genomic_DNA.
DR RefSeq; WP_011054062.1; NC_004061.1.
DR AlphaFoldDB; Q9Z617; -.
DR SMR; Q9Z617; -.
DR STRING; 198804.BUsg_558; -.
DR EnsemblBacteria; AAM68096; AAM68096; BUsg_558.
DR KEGG; bas:BUsg_558; -.
DR eggNOG; COG1220; Bacteria.
DR HOGENOM; CLU_033123_0_0_6; -.
DR OMA; KYGMIKT; -.
DR OrthoDB; 718259at2; -.
DR Proteomes; UP000000416; 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.
FT CHAIN 1..443
FT /note="ATP-dependent protease ATPase subunit HslU"
FT /id="PRO_0000160487"
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; 50030 MW; 914E269263FB8DB1 CRC64;
MSEMTPPQIV SELNKFIIGQ EQAKKAVAIA LRNRWRRMQL NNELRHEITP KNILMIGPTG
VGKTEIARRL AKLANSPFIK VEATKFTEVG YVGKEVDSII RDLTDAAIKM IRVKNIEKNK
LRVEEIVEER ILDVLVPRPK NNWTENEKNE SLLNTLQVFR KKLREGILDE KEIEINVLAS
TMGVEIMAPP GMEELTSQLQ SLFQNLGGHK KNTRRLKIKD AVLLLKEEEA AKLINQEEIK
KEAINAVEQN GIVFVDEIDK ICKRRDSSGP DVSREGVQRD LLPLVEGCTV STKYGMVKTD
HILFIASGAF QTSTPSDLIP ELQGRLPIKV ELQPLTINDF EKILTEPTAS ITAQYKALMK
TEGVCINFTK EGIRNIAEAA WKVNESMENI GARRLHTILE KLMEDISFNA CDNVGKTIEI
NSEYVGKHLD QLISNEDLGR FIL