ID   HSLU_VIBPA              Reviewed;         443 AA.
AC   Q87T21;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=VP0249;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC58512.1; -; Genomic_DNA.
DR   RefSeq; NP_796628.1; NC_004603.1.
DR   RefSeq; WP_005457198.1; NC_004603.1.
DR   AlphaFoldDB; Q87T21; -.
DR   SMR; Q87T21; -.
DR   STRING; 223926.28805231; -.
DR   PRIDE; Q87T21; -.
DR   EnsemblBacteria; BAC58512; BAC58512; BAC58512.
DR   GeneID; 1187716; -.
DR   KEGG; vpa:VP0249; -.
DR   PATRIC; fig|223926.6.peg.241; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_6; -.
DR   OMA; KYGMIKT; -.
DR   Proteomes; UP000002493; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..443
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_0000160559"
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;  49880 MW;  B68CA48391AFD9BF CRC64;
     MSEMTPREIV HELNRHIIGQ DKAKRSVAIA LRNRWRRMQL EESLRVEVTP KNILMIGPTG
     VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVETII RDLTDVAVKM THQQAMEKVK
     FRAEEQAEER ILDALLPPAR DSWGQVEQKE DTSNTRQIFR KKLREGQLDD KEIEIDVAAP
     QMGVEIMAPP GMEEMTNQLQ GMFQNLAGDT KKKRKLKIKD AMKALAEEEA AKLVNQEELK
     EAAIFNVENN GIVFIDEIDK ICKRGESSGP DVSREGVQRD LLPLIEGSTV STKHGMVKTD
     HILFVASGAF QVAKPSDLIP ELQGRLPIRV ELEALSSNDF KRILTEPKAS LTEQYIALMK
     TEDVDIEFTE DGITRIAEAA WTVNETTENI GARRLHTVME RLMDEISYDA AEQSGAKFVI
     DAAYVQARLG DTIEDEDLSR FIL