ID W8F1H4_9BACT Unreviewed; 471 AA.
AC W8F1H4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=Hsw_3168 {ECO:0000313|EMBL:AHJ98763.1};
OS Hymenobacter swuensis DY53.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ98763.1, ECO:0000313|Proteomes:UP000019423};
RN [1] {ECO:0000313|EMBL:AHJ98763.1, ECO:0000313|Proteomes:UP000019423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY53 {ECO:0000313|EMBL:AHJ98763.1,
RC ECO:0000313|Proteomes:UP000019423};
RA Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT "Complete genome sequence of ionizing-radiation resistance bacterium
RT Hymenobacter swuensis DY53.";
RL Submitted (JAN-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP007145; AHJ98763.1; -; Genomic_DNA.
DR RefSeq; WP_044002876.1; NZ_CP007145.1.
DR AlphaFoldDB; W8F1H4; -.
DR STRING; 1227739.Hsw_3168; -.
DR KEGG; hsw:Hsw_3168; -.
DR PATRIC; fig|1227739.3.peg.3339; -.
DR eggNOG; COG1220; Bacteria.
DR HOGENOM; CLU_033123_0_0_10; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000019423; 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 CDD; cd19498; RecA-like_HslU; 1.
DR Gene3D; 1.10.8.60; -; 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 Pfam; PF10431; ClpB_D2-small; 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, ECO:0000313|EMBL:AHJ98763.1};
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:AHJ98763.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:AHJ98763.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019423}.
FT DOMAIN 53..358
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 361..457
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT BINDING 22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 64..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 419
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 471 AA; 52372 MW; F9E71048B30676F4 CRC64;
MLDSAEFLTP AQIVAELDKY IIGQHEAKRY VAIALRNRWR RLHAAPDMQR EIVPNNILMI
GSTGVGKTEI ARRLASISGA PFTKVEASKF TEVGYVGRDV ESMVRDLVEQ SVNMVKLRRK
EEVKAQAAQA VEDLILDILI PPVTNAAQPA AKPTLGFPVA APCEMPDSDH ELNERTRERF
REKIRNGELD ERKIEIRVQH TSGPGISVMG GPGGMDEASM AGIQDMLGSM LPKKTRKRKV
TVAEARKILL DEEAAKLIDM DEVKDEAIRQ AENAGIIFID EIDKVASRSG KGGSGPDVSR
EGVQRDLLPI VEGSAVNTKY GIIQTDHILF IAAGAFHVAK PSDLIPELQG RFPIRVELQS
LTKEDFFRIL KDPKNALTKQ YEALLQAEGV VLTFDDAALE RLAEIAFEVN SEVENIGARR
LHTVMSRLLN DILFDVPDRI GPNAHILITL ELVEERLRDM VRNRDLSQYI L
//