ID   HSLU_SHEAM              Reviewed;         441 AA.
AC   A1S2P4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Sama_0440;
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
RL   Submitted (DEC-2006) 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; CP000507; ABL98650.1; -; Genomic_DNA.
DR   RefSeq; WP_011758560.1; NC_008700.1.
DR   AlphaFoldDB; A1S2P4; -.
DR   SMR; A1S2P4; -.
DR   STRING; 326297.Sama_0440; -.
DR   PRIDE; A1S2P4; -.
DR   EnsemblBacteria; ABL98650; ABL98650; Sama_0440.
DR   KEGG; saz:Sama_0440; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_6; -.
DR   OMA; KYGMIKT; -.
DR   OrthoDB; 718259at2; -.
DR   Proteomes; UP000009175; 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   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..441
FT                   /note="ATP-dependent protease ATPase subunit HslU"
FT                   /id="PRO_1000012799"
FT   REGION          137..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
FT   BINDING         391
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   441 AA;  49754 MW;  B6608D9CC0941620 CRC64;
     MSEMTPREIV HELDAHIIGQ QKAKRSVAVA LRNRWRRMQL DAALRHEVTP KNILMIGPTG
     VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVEQII RDLTDTAIKL TREVEMKKCR
     TRAEEAAEER VLDALLPRPK NDWDNNSDDN SSSRQIFRKK LREGQLDDKE IEIDIAGPQI
     GVEIMSPPGM EEMTNQLQSL FQNMGQAPAK RKKMKIKEAL KQLVDEEAAK LVNQEDLKEK
     AIELVEQHGI VFIDEIDKIC KRGETSGPDV SREGVQRDLL PLVEGCTVNT KHGMVKTDHI
     LFIASGAFQM SKPSDLIPEL QGRLPIRVEL DALTASDFKR ILTEPHASLT EQYVALMATE
     GVTIEFTETG IDRIAQAAWQ VNERTENIGA RRLHTVMERL MEDISFEASD KSGSKFTIDA
     DYVNAHLDNL VQDEDLSRFI L