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Database: UniProt
Entry: A0A0X8D3P1_9BACL
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ID   A0A0X8D3P1_9BACL        Unreviewed;       474 AA.
AC   A0A0X8D3P1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=ACH33_07220 {ECO:0000313|EMBL:AMA72661.1};
OS   Aneurinibacillus sp. XH2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA72661.1, ECO:0000313|Proteomes:UP000065566};
RN   [1] {ECO:0000313|Proteomes:UP000065566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xh2 {ECO:0000313|Proteomes:UP000065566};
RA   Xi L.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMA72661.1, ECO:0000313|Proteomes:UP000065566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xh2 {ECO:0000313|EMBL:AMA72661.1,
RC   ECO:0000313|Proteomes:UP000065566};
RA   Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT   "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT   Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao oilfield in
RT   China.";
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}.
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DR   EMBL; CP014140; AMA72661.1; -; Genomic_DNA.
DR   RefSeq; WP_057898398.1; NZ_CP014140.1.
DR   AlphaFoldDB; A0A0X8D3P1; -.
DR   STRING; 1450761.ACH33_07220; -.
DR   KEGG; anx:ACH33_07220; -.
DR   Proteomes; UP000065566; 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:AMA72661.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:AMA72661.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065566}.
FT   DOMAIN          60..363
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          366..460
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         71..76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         288
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         424
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   474 AA;  53511 MW;  8EF4A1AD72E71BAE CRC64;
     MNDEEAVPLK NPERLTPKQI VEQLDHFIVG QKQAKRSVAI ALRNRYRRSL LPEEIRDEIV
     PKNILMIGPT GVGKTEIARR LAKLTGAPFI KVEATKFTEV GYVGRDVESM VRDLVETAIR
     MVKAEKTEQV KDKAEAMANE RIVHILVPGK HANKSFKNPL EMLFGGNQNT YQSATGDADD
     LSVSQQRRQV AHQLAMGQLE DTVIEIEVED TAPTMFDMFS GSGMDQMGIN MQEMLGSLLP
     KRMKKRKLPI REARKVLIMQ EAQKLIDMDE VIQESIERAE QSGIIFIDEI DKIAGKETNS
     AQVSREGVQR DILPIVEGST VMTKYGPVKT DYILFIAAGA FHMAKPSDLI PELQGRFPIR
     VELDSLRVED FVQILTEPKN ALIKQYVSLL ETEGIKVEFS DEAIKEIAKL AAEVNQNTDN
     IGARRLHTIM EKLLEDLSFE ASDITLEKVV ITPEYVREKL KDIVEDRDLS RYIL
//
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