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Database: UniProt
Entry: A0A0D8I6X3_9CLOT
LinkDB: A0A0D8I6X3_9CLOT
Original site: A0A0D8I6X3_9CLOT 
ID   A0A0D8I6X3_9CLOT        Unreviewed;       463 AA.
AC   A0A0D8I6X3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, 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   ECO:0000313|EMBL:AKL95490.1};
GN   ORFNames=CACET_c20420 {ECO:0000313|EMBL:AKL95490.1};
OS   Clostridium aceticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL95490.1, ECO:0000313|Proteomes:UP000035704};
RN   [1] {ECO:0000313|EMBL:AKL95490.1, ECO:0000313|Proteomes:UP000035704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL95490.1,
RC   ECO:0000313|Proteomes:UP000035704};
RA   Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., Daniel R.;
RT   "Genome sequence of Clostridium aceticum DSM 1496.";
RL   Submitted (OCT-2014) 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; CP009687; AKL95490.1; -; Genomic_DNA.
DR   RefSeq; WP_044826007.1; NZ_JYHU01000021.1.
DR   AlphaFoldDB; A0A0D8I6X3; -.
DR   STRING; 84022.CACET_c20420; -.
DR   KEGG; cace:CACET_c20420; -.
DR   PATRIC; fig|84022.5.peg.1847; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000035704; 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: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};
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:AKL95490.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:AKL95490.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035704}.
FT   DOMAIN          49..356
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          355..449
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         276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   463 AA;  52671 MW;  8EF27E386AA1ABDB CRC64;
     MKEFTPRQVV EELDKYIIGQ QEAKKAVAIA LRNRIRRSKI SIEFQEEIKP KNILMIGPTG
     VGKTEIARRL AKLIDAPFIK VEATKFTEVG YVGRDVESMI RDLVEASIRI IKGKHIEKNY
     EKAKKLANHR LLDLLDPTPR KETSFKNPFD MLFKTSHNEE ESTSEKEHEV DLKLKRQQIE
     KQLTEGLLEN ELVEVEIEDR MPNTFEIFGA GNEEMNINLQ DMLGGIIPKK TKKRKVTVSE
     ARKILIEEEA QKLVDMDEVI ATAINNAEQQ GIIFIDEIDK IAGGHGGSGP DVSREGVQRD
     ILPIIEGSTV MTKYGPVKTD HILFIAAGAF HIAKVSDLIP ELQGRFPIRV NLSNLTIEDF
     KKILTQPQNA LLTQYKLLLE TEGIKIHFLE EAIDEIAMVS YMTNEQGDNI GARRLHTITE
     KLLEDISFEA PELSEKEITI DQQYVKKKLN NTVKTFSEDK YII
//
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