ID H0UKL3_9BACT Unreviewed; 462 AA.
AC H0UKL3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=ATP-dependent protease ATPase subunit HslU {ECO:0000256|HAMAP-Rule:MF_00249};
DE AltName: Full=Unfoldase HslU {ECO:0000256|HAMAP-Rule:MF_00249};
GN Name=hslU {ECO:0000256|HAMAP-Rule:MF_00249};
GN ORFNames=JonanDRAFT_0847 {ECO:0000313|EMBL:EHM13222.1};
OS Jonquetella anthropi DSM 22815.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Jonquetella.
OX NCBI_TaxID=885272 {ECO:0000313|EMBL:EHM13222.1, ECO:0000313|Proteomes:UP000003806};
RN [1] {ECO:0000313|EMBL:EHM13222.1, ECO:0000313|Proteomes:UP000003806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22815 {ECO:0000313|EMBL:EHM13222.1,
RC ECO:0000313|Proteomes:UP000003806};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The Noncontiguous Finished genome of Jonquetella anthropi DSM 22815.";
RL Submitted (NOV-2011) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_00249}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.
CC {ECO:0000256|ARBA:ARBA00009771, ECO:0000256|HAMAP-Rule:MF_00249}.
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DR EMBL; CM001376; EHM13222.1; -; Genomic_DNA.
DR RefSeq; WP_008521218.1; NZ_CM001376.1.
DR AlphaFoldDB; H0UKL3; -.
DR STRING; 885272.JonanDRAFT_0847; -.
DR eggNOG; COG1220; Bacteria.
DR HOGENOM; CLU_033123_0_0_0; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000003806; 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:UniProtKB-KW.
DR GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00390; hslU; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR48102:SF3; ATP-DEPENDENT PROTEASE ATPASE SUBUNIT HSLU; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00249};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249};
KW Hydrolase {ECO:0000313|EMBL:EHM13222.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:EHM13222.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003806}.
FT DOMAIN 55..351
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 354..450
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 66..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 462 AA; 51202 MW; DDC14CBBC17F7A02 CRC64;
MAEIYNADSL QPAAIVAYLD RYIVGQTEAK RAVAVALRNR VRRRRLPEEL AAEITPKNIL
MVGPTGVGKT EIARRLASLV QAPFVKVEAT KFTEVGYVGR DVESMVRDLV EAAVRMVKER
MAAEKTDSAA SAARERMIDY LVPVKRSGEG GGIPTFMSYL KGVEADEPSQ GPEMKDSTRD
KMRRLLEEGK LDDREVEIEV QETPPATGMD QSAMGVNIGE MLGSFMPKRT KRRRVKVKDG
LRILQAEEAE KLIDTDRAHQ EAIKSAQDEG IIFIDEIDKV VASENRGGAD VSREGVQRDL
LPIVEGCTVP TKYGPVKTDH MLFIAAGAFQ SVKPSDLVPE LQGRLPLRVE LSALRKEDLS
KILTEPRHNL LDQYKALLST EGVELCFTAD GIDRLAELAE RTNRESENIG ARRLHTMLER
VLEDVSFSAS DYAGQTVTID RAAVDKKLAD IAANVDLRRY LL
//
