HSLU_SALTY
ID HSLU_SALTY Reviewed; 443 AA.
AC O30911; Q9K4Q5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
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=STM4091;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chiang Y.L.;
RL Thesis (2000), National Taiwan University, Taiwan.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-300.
RX PubMed=9302299; DOI=10.1126/science.277.5334.2007;
RA Valdivia R.H., Falkow S.;
RT "Fluorescence-based isolation of bacterial genes expressed within host
RT cells.";
RL Science 277:2007-2011(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 -!- 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; AJ295710; CAC00720.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22931.1; -; Genomic_DNA.
DR EMBL; AF020812; AAB80745.1; -; Genomic_DNA.
DR RefSeq; NP_462972.1; NC_003197.2.
DR RefSeq; WP_001293360.1; NC_003197.2.
DR AlphaFoldDB; O30911; -.
DR SMR; O30911; -.
DR STRING; 99287.STM4091; -.
DR PaxDb; O30911; -.
DR EnsemblBacteria; AAL22931; AAL22931; STM4091.
DR GeneID; 1255618; -.
DR KEGG; stm:STM4091; -.
DR PATRIC; fig|99287.12.peg.4312; -.
DR HOGENOM; CLU_033123_0_0_6; -.
DR OMA; KYGMIKT; -.
DR PhylomeDB; O30911; -.
DR BioCyc; SENT99287:STM4091-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0009376; C:HslUV protease complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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 GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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; Reference proteome;
KW Stress response.
FT CHAIN 1..443
FT /note="ATP-dependent protease ATPase subunit HslU"
FT /id="PRO_0000160543"
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 CONFLICT 185
FT /note="E -> K (in Ref. 3; AAB80745)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="A -> P (in Ref. 3; AAB80745)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="K -> N (in Ref. 3; AAB80745)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 49668 MW; 8CBB418D0DCACD4E CRC64;
MSEMTPREIV SELNKHIIGQ DNAKRSVAIA LRNRWRRMQL DEELRHEVTP KNILMIGPTG
VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDAAVKM VRVQAIEKNR
YRAEELAEER ILDVLIPPAK NNWGQAEQQQ EPSAARQTFR KKLREGQLDD KEIEINLAAA
PMGVEIMAPP GMEEMTSQLQ SMFQNLGGQK QKPRKLKIKD AMKLLVEEEA AKLVNPEELK
QDAIDAVEQH GIVFIDEIDK ICKRGETSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD
HILFIASGAF QVAKPSDLIP ELQGRLPIRV ELQALTTSDF ERILTEPNAS VTVQYKALMA
TEGVNIEFTD SGIKRIAEAA WQVNETTENI GARRLHTVLE RLMEEISYNA SDLHGQNITI
DAEYVSKHLD ALVADEDLSR FIL
