HSLU_ECO57
ID HSLU_ECO57 Reviewed; 443 AA.
AC P0A6H6; P32168;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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}; Synonyms=htpI;
GN OrderedLocusNames=Z5478, ECs4858;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG59126.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38281.1; -; Genomic_DNA.
DR PIR; B86083; B86083.
DR PIR; B91236; B91236.
DR RefSeq; NP_312885.1; NC_002695.1.
DR RefSeq; WP_001293341.1; NZ_SWKA01000005.1.
DR PDB; 5JI2; X-ray; 3.31 A; E/F=2-443.
DR PDBsum; 5JI2; -.
DR AlphaFoldDB; P0A6H6; -.
DR SMR; P0A6H6; -.
DR STRING; 155864.EDL933_5262; -.
DR EnsemblBacteria; AAG59126; AAG59126; Z5478.
DR EnsemblBacteria; BAB38281; BAB38281; ECs_4858.
DR GeneID; 58459844; -.
DR GeneID; 915031; -.
DR KEGG; ece:Z5478; -.
DR KEGG; ecs:ECs_4858; -.
DR PATRIC; fig|386585.9.peg.5080; -.
DR eggNOG; COG1220; Bacteria.
DR HOGENOM; CLU_033123_0_0_6; -.
DR OMA; KYGMIKT; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..443
FT /note="ATP-dependent protease ATPase subunit HslU"
FT /id="PRO_0000160501"
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"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:5JI2"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 21..38
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 98..135
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 236..250
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 269..286
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:5JI2"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 370..386
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 393..409
FT /evidence="ECO:0007829|PDB:5JI2"
FT TURN 410..415
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 422..434
FT /evidence="ECO:0007829|PDB:5JI2"
FT HELIX 436..442
FT /evidence="ECO:0007829|PDB:5JI2"
SQ SEQUENCE 443 AA; 49594 MW; D2188639EA9AEF4C 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
TEGVNIEFTD SGIKRIAEAA WQVNESTENI GARRLHTVLE RLMEEISYDA SDLSGQNITI
DADYVSKHLD ALVADEDLSR FIL
