ID A0A5D0CWP1_9BACL Unreviewed; 469 AA.
AC A0A5D0CWP1;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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:TYA14362.1};
GN ORFNames=FRY98_01335 {ECO:0000313|EMBL:TYA14362.1};
OS Paenibacillus faecis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=862114 {ECO:0000313|EMBL:TYA14362.1, ECO:0000313|Proteomes:UP000325218};
RN [1] {ECO:0000313|EMBL:TYA14362.1, ECO:0000313|Proteomes:UP000325218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23593 {ECO:0000313|EMBL:TYA14362.1,
RC ECO:0000313|Proteomes:UP000325218};
RA Kook J.-K., Park S.-N., Lim Y.K.;
RT "Genome sequencing of Paenibacillus faecis DSM 23593(T).";
RL Submitted (AUG-2019) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TYA14362.1}.
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DR EMBL; VSDO01000001; TYA14362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D0CWP1; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000325218; Unassembled WGS sequence.
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; 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:TYA14362.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:TYA14362.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000325218}.
FT DOMAIN 51..358
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 361..455
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 154..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 62..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 282
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 469 AA; 52561 MW; 10D8F07C4F34F6EF CRC64;
MPNANLTPRQ IVAELDKYIV GQKQAKKSVA VALRNRYRRS LLSEDVQDEI VPKNILMIGP
TGVGKTEIAR RLAKLVGAPF IKVEATKFTE VGYVGRDVES MVRDLVETAI RTVKLERTEK
VKDKAEELAN ERLVHILVPS PNKSKNSRNP FEMLFGNQNA GETSGASQEK SEEDGDLAER
RRQVRFKLLA GQLENDIVEI EVEDNAPTMM DMFAGQGNDQ MGMNMQEMFG NLLPRRTKRR
KLSIKEARKV LTQEEASKLI DHDDLVQEAV ERAEQTGIIF IDEIDKVASR GQGSGPDVSR
EGVQRDILPI VEGSTVMTKY GPVKTDYILF IAAGAFHIAK PSDLIPELQG RFPIRVELSS
LSLDDFVSIL TEPQNALTKQ YTELLRTEDI EIEFSSEAIR EIAAIAASVN ANTENIGARR
LHTILEKLLE DLSFEAPELT LEKMTITPEY VREKLGDIAK DRDLSQYIL
//