ID F8IHW8_ALIAT Unreviewed; 466 AA.
AC F8IHW8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 ECO:0000313|EMBL:AEJ43258.1};
GN OrderedLocusNames=TC41_1320 {ECO:0000313|EMBL:AEJ43258.1};
OS Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus acidocaldarius).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1048834 {ECO:0000313|EMBL:AEJ43258.1, ECO:0000313|Proteomes:UP000000292};
RN [1] {ECO:0000313|EMBL:AEJ43258.1, ECO:0000313|Proteomes:UP000000292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tc-4-1 {ECO:0000313|EMBL:AEJ43258.1,
RC ECO:0000313|Proteomes:UP000000292};
RX PubMed=21914900; DOI=10.1128/JB.05709-11;
RA Chen Y., He Y., Zhang B., Yang J., Li W., Dong Z., Hu S.;
RT "Complete Genome Sequence of Alicyclobacillus acidocaldarius Strain Tc-
RT 4-1.";
RL J. Bacteriol. 193:5602-5603(2011).
RN [2] {ECO:0000313|Proteomes:UP000000292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tc-4-1 {ECO:0000313|Proteomes:UP000000292};
RA Chen Y., He Y., Dong Z., Hu S.;
RT "The complete genome sequence of Alicyclobacillus acidocaldarius sp. Tc-4-
RT 1.";
RL Submitted (JUN-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; CP002902; AEJ43258.1; -; Genomic_DNA.
DR AlphaFoldDB; F8IHW8; -.
DR STRING; 1048834.TC41_1320; -.
DR KEGG; aad:TC41_1320; -.
DR PATRIC; fig|1048834.4.peg.1257; -.
DR eggNOG; COG1220; Bacteria.
DR HOGENOM; CLU_033123_0_0_9; -.
DR Proteomes; UP000000292; 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 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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00249};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00249};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Stress response {ECO:0000313|EMBL:AEJ43258.1}.
FT DOMAIN 54..355
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 358..457
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT BINDING 23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 65..70
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 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 466 AA; 52474 MW; 3378BE1BEAEE970F CRC64;
MAMPSERELT PREIVEYLDR YIVGQKKAKR AVAIALRNRY RRSKLSPEMQ AEVTPKNILM
IGPTGVGKTE IARRLSKLVG APFIKVEATK FTEVGYVGRD VESMVRDLVE TAVRMVKAEH
AERVKSEAEA RANDRIVEAL VPDPGARSRA RNPFEMLFSG GFASERPQEP SSDQIREERR
RVKQKLLMGA LEDHYVEVDV EEQAGPMALG FIPGMGAESL GNLQEMLGNL LPKSTKKRKM
TVREARKVLT QEEAQKLIDM DAVTAEAIYR AENHGIIFID EMDKIAGRET HGPDVSREGV
QRDILPIVEG STVSTKYGAV KTDYMLFIGA GAFHVAKPSD LIPELQGRFP IRVELEPLTK
EDFVRILREP ENSLIKQYTA LLETEGVRVE FTDEAIERIA EMAQKVNEET ENIGARRLHT
LVEKVLEDLS FEAPEIHLGE IKITRAYVDE KLGDIVQNRD LSQFIL
//
