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Database: UniProt
Entry: A0A1Q8QPU4_9FIRM
LinkDB: A0A1Q8QPU4_9FIRM
Original site: A0A1Q8QPU4_9FIRM 
ID   A0A1Q8QPU4_9FIRM        Unreviewed;       461 AA.
AC   A0A1Q8QPU4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=DSOL_3635 {ECO:0000313|EMBL:OLN29298.1};
OS   Desulfosporosinus metallidurans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1888891 {ECO:0000313|EMBL:OLN29298.1, ECO:0000313|Proteomes:UP000186102};
RN   [1] {ECO:0000313|EMBL:OLN29298.1, ECO:0000313|Proteomes:UP000186102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OL {ECO:0000313|EMBL:OLN29298.1,
RC   ECO:0000313|Proteomes:UP000186102};
RA   Mardanov A., Beletsky A., Panova A., Karnachuk O., Ravin N.;
RT   "Complete genome of Desulfosporosinus sp. OL.";
RL   Submitted (SEP-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:OLN29298.1}.
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DR   EMBL; MLBF01000034; OLN29298.1; -; Genomic_DNA.
DR   RefSeq; WP_075366090.1; NZ_MLBF01000034.1.
DR   AlphaFoldDB; A0A1Q8QPU4; -.
DR   STRING; 1888891.DSOL_3635; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000186102; 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   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:OLN29298.1};
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:OLN29298.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:OLN29298.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186102}.
FT   DOMAIN          49..349
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          352..447
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         60..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         273
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         410
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   461 AA;  51860 MW;  69AF02A3BA9979A3 CRC64;
     MDHLTPREIV RELDRDIVGQ NAAKRAVAVA LRNRYRRSCL PEQLQEEIIP KNILMIGPTG
     VGKTEIARRL AKLVRAPFIK IEATKFTEVG YVGRDVEAII RDLVEISLRM VKAERTEQVQ
     AQAAVNAEKR LVELLVPEKR SESSSSNPFQ MLFGQASDQE KKIEVSPQIE QERKLVAEHL
     RLGELEERVI EISVEESTPL SDMLGNNNMM EMGLNIQDMM SGLLPKKHKN RKVTVREARK
     ILIHEEAQNL IDQEEAVQEA IRRTEHEGIV FLDEIDKIAG REGAGGPDVS RGGVQRDILP
     IVEGSTVVTK YGPVKTDHIL FIAAGAFHLS KPSDLIPELQ GRFPIRVELE SLSVADFKRI
     LTEPQSSLIK QYSALLGTEG IKVDFTENAI DELAEVAYQV NSTAENIGAR RLHTIVEKVL
     EELSFEASEL PDDYTVTINR EYVQQRLGNV VQNQDLARYI L
//
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