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Database: UniProt
Entry: A0A286U1M7_9BACT
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Original site: A0A286U1M7_9BACT 
ID   A0A286U1M7_9BACT        Unreviewed;       457 AA.
AC   A0A286U1M7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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:GAX62027.1};
GN   ORFNames=SCALIN_C28_0229 {ECO:0000313|EMBL:GAX62027.1};
OS   Candidatus Scalindua japonica.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Scalinduaceae; Candidatus Scalindua.
OX   NCBI_TaxID=1284222 {ECO:0000313|EMBL:GAX62027.1, ECO:0000313|Proteomes:UP000218542};
RN   [1] {ECO:0000313|Proteomes:UP000218542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=husup-a2 {ECO:0000313|Proteomes:UP000218542};
RA   Oshiki M., Mizuto K., Kimura Z., Kindaichi T., Satoh H., Okabe S.;
RT   "Genetic Diversity of Marine Anaerobic Ammonium-Oxidizing Bacteria as
RT   Revealed by Genomic and Proteomic Analyses of 'Candidatus Scalindua
RT   japonica'.";
RL   Environ. Microbiol. Rep. 0:0-0(2017).
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:GAX62027.1}.
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DR   EMBL; BAOS01000028; GAX62027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286U1M7; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000218542; 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; 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   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218542};
KW   Stress response {ECO:0000313|EMBL:GAX62027.1}.
FT   DOMAIN          49..346
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          349..448
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         270
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         407
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   457 AA;  52107 MW;  83B8684A7A6C43ED CRC64;
     MRELTPRKIV EELDKYIVGQ KEAKRAVAIA IRNRWRRLQL SDELREEVMP KNIIMIGPTG
     VGKTEIARRI ANLVKAPFLK VEASKYTEVG YHGRDVESMI RDIVEIAVNM VRTEQMEKVS
     VKADMNTEER LLDLLLPLPE AKEEVAVVRG EGEDRDVDKG GTVVEKRETT REKFRNKLRQ
     GKLEDRMVEI KTQEKPVVMQ GIVAGIEEIG VDFQNVIEKM IPPKTQVKKT PISDARKIIK
     QEEAEKLIDK EKVTKDALHR AENMGIVFID ELDKVASRES GHGPDISREG VQRDILPIVE
     GSTVVTRYGM VKTDRILFIA AGAFHVSKPS DLIPELQGRF PIRVELKDLG KEEFIRILTE
     PKNALIKQYT ELLKTEKVNL QFNKDAIEEI TDVAVKINKR SQSIGARRLH TVMEKLLEDA
     SFDAPDLDDK NIVVDAEYVQ DKMKDIVKDE DLTKYIL
//
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