ID A0A133S8T8_9FIRM Unreviewed; 465 AA.
AC A0A133S8T8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=HMPREF3201_02440 {ECO:0000313|EMBL:KXA66101.1};
OS Megasphaera sp. MJR8396C.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1603888 {ECO:0000313|EMBL:KXA66101.1, ECO:0000313|Proteomes:UP000070314};
RN [1] {ECO:0000313|EMBL:KXA66101.1, ECO:0000313|Proteomes:UP000070314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR9396C {ECO:0000313|EMBL:KXA66101.1,
RC ECO:0000313|Proteomes:UP000070314};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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:KXA66101.1}.
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DR EMBL; LRVC01000114; KXA66101.1; -; Genomic_DNA.
DR RefSeq; WP_062413128.1; NZ_KQ958211.1.
DR AlphaFoldDB; A0A133S8T8; -.
DR STRING; 1603888.HMPREF3201_02440; -.
DR PATRIC; fig|1603888.3.peg.2348; -.
DR Proteomes; UP000070314; 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; 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 Hydrolase {ECO:0000313|EMBL:KXA66101.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:KXA66101.1}.
FT DOMAIN 51..354
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 357..453
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT REGION 155..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 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ SEQUENCE 465 AA; 52707 MW; AA33875F2AFBB72B CRC64;
MEQSSWTPKQ IVAELNKYIV GQGDAKKSVA IALRNRWRRK RLSEEMQDEI IPKNILLIGP
TGVGKTEIAR RLAKLVGAPF IKVEATKYTE VGYVGRDVEQ MIRDLVANAI RMVQEQESQR
YEEKAEAEAN KRILQVFWPK KSVVEKVKNP MDVFFGSDDD ETKEEPKQLE EGNSDRRQKM
LEDICAHKMD DREIEVEVAE QGPGFQGILT GNSTEELTNN FQEMLGSIMP KKKKKKKMTV
AKAREIFKEE ELEKCLDMDT IVDKAVAATE ESGIVFIDEF DKIAEKGRTN GPDVSREGVQ
RDILPIVEGA TVNTKYGPVK TDHILFIAAG AFHVSKPSDL IPELQGRFPI RVELQSLTVE
DFRRILTEPS QSLVKQYTAL LETEGLTLDF TDDGINAIAE YAYRVNRETE NIGARRLHTI
LEKILEDVAY EAPDVDEKNI VIDKDFVAGK LHDVVQNVDL SHYIL
//
