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Database: UniProt
Entry: A0A127AYU3_9BACT
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ID   A0A127AYU3_9BACT        Unreviewed;       469 AA.
AC   A0A127AYU3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=TH61_01955 {ECO:0000313|EMBL:AMM50185.1};
OS   Rufibacter sp. DG15C.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Rufibacter.
OX   NCBI_TaxID=1379909 {ECO:0000313|EMBL:AMM50185.1, ECO:0000313|Proteomes:UP000070672};
RN   [1] {ECO:0000313|EMBL:AMM50185.1, ECO:0000313|Proteomes:UP000070672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG15C {ECO:0000313|EMBL:AMM50185.1,
RC   ECO:0000313|Proteomes:UP000070672};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Rufibacter sp. DG15C whole genome sequencing.";
RL   Submitted (JAN-2015) 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; CP010776; AMM50185.1; -; Genomic_DNA.
DR   RefSeq; WP_066505159.1; NZ_CP010776.1.
DR   AlphaFoldDB; A0A127AYU3; -.
DR   STRING; 1379909.TH61_01955; -.
DR   KEGG; rud:TH61_01955; -.
DR   PATRIC; fig|1379909.4.peg.420; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000070672; 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   Pfam; PF10431; ClpB_D2-small; 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:AMM50185.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:AMM50185.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070672}.
FT   DOMAIN          53..356
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          359..455
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         64..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         417
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   469 AA;  52276 MW;  68D2CC6D628B415F CRC64;
     MLDPTKYLTP AQIVAELDKY IIGQHDAKRN VAIALRNRWR RMHADPEMQK EIVPNNILMI
     GATGVGKTEI ARRLASIADA PFTKVEASKF TEVGYIGRDV ESMVRDLVEQ AVNMVKTRKK
     EEVKTQAAQM VEDIILDALI PPINQSGGGN GMLGFGGSSN STSDVPDNDY ELNERTRERF
     REKIRNGELE DRKIEIKVAH NPSSGVGVMG PGMDEMQMAG IQEMIGNMMP KKTKKRKVTI
     SEARKILLEE EASKLIDMDE VKEEAIAKAE NAGVIFIDEI DKVASASGKG GSGPDVSREG
     VQRDLLPIVE GSTVNTKYGV IKTDHILFIA AGAFHVAKPS DLIPELQGRF PIRVELQSLS
     KDDFYQILKY PKNALTKQYV ELLRAEEVEL SFSDEALHKI AEIAFEVNAE VENIGARRLH
     TVMSRLLNDI LYDVPDTIPA NARLLVTPEL VEERLRDMVK NRDLSQYIL
//
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