ID A0A4Y8LKI2_9BACL Unreviewed; 469 AA.
AC A0A4Y8LKI2;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-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:TFE03506.1};
GN ORFNames=E2491_01565 {ECO:0000313|EMBL:TFE03506.1};
OS Jeotgalibacillus sp. R-1-5s-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=2555897 {ECO:0000313|EMBL:TFE03506.1, ECO:0000313|Proteomes:UP000297458};
RN [1] {ECO:0000313|EMBL:TFE03506.1, ECO:0000313|Proteomes:UP000297458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-1-5s-1 {ECO:0000313|EMBL:TFE03506.1,
RC ECO:0000313|Proteomes:UP000297458};
RA Yang Y.;
RL Submitted (MAR-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:TFE03506.1}.
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DR EMBL; SORW01000002; TFE03506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y8LKI2; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000297458; 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: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; IPR001270; ClpA/B.
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 PRINTS; PR00300; CLPPROTEASEA.
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 Reference proteome {ECO:0000313|Proteomes:UP000297458}.
FT DOMAIN 51..362
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 REGION 153..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..168
FT /note="Polar residues"
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 281
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; 52891 MW; 8C1B47D8F89603A6 CRC64;
MSTVELTPKQ IVEKLDQYIV GQRDAKRAVA VALRNRYRRN LLDESLRNEV IPKNILMMGP
TGVGKTEIAR RIAKLVGAPF VKVEATKFTE VGYVGRDVES MVRDLMETSV RIVKEEKMQS
VQEKAEENAN KRIVKLLVPS AKKTQNFKNP FEMMFGNSDQ NQNDAQDQQD DESALKDKRR
EIADKLKNGQ LEERIITVEV DEQQSASMYD MLQGSGMEQM GMNFQDALSN LMPKKKKKRK
LTVKEARKVL THDEAVKLID MDEVAQAALY RAEQMGIIFI DEIDKIASKS SGSGSADVSR
EGVQRDILPI VEGSTVNTKY GPVKTDHVLF VAAGAFHMSK PSDLIPELQG RFPIRVELQK
LTVEDFVRIM VEPDHALIKQ YKALLETEGI QVDFTEDAIR RLAEIAYTVN QETDNIGARR
LHTIMEKLLE DLSFEASDIQ LGTISITPAY VDEKLGAIAK NRDLSEFIL
//