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
//