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Entry: A0A075WW98_9BACT
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ID   A0A075WW98_9BACT        Unreviewed;       442 AA.
AC   A0A075WW98;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   08-NOV-2023, entry version 46.
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=HL41_09065 {ECO:0000313|EMBL:AIH04778.1};
OS   Thermodesulfobacterium commune DSM 2178.
OC   Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC   Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC   Thermodesulfobacterium.
OX   NCBI_TaxID=289377 {ECO:0000313|EMBL:AIH04778.1, ECO:0000313|Proteomes:UP000028481};
RN   [1] {ECO:0000313|EMBL:AIH04778.1, ECO:0000313|Proteomes:UP000028481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2178 {ECO:0000313|EMBL:AIH04778.1,
RC   ECO:0000313|Proteomes:UP000028481};
RX   PubMed=25635017;
RA   Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA   Robb F.T., Ward N.L., Eisen J.A.;
RT   "Genome Sequence of a Sulfate-Reducing Thermophilic Bacterium,
RT   Thermodesulfobacterium commune DSM 2178T (Phylum Thermodesulfobacteria).";
RL   Genome Announc. 3:0-0(2015).
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; CP008796; AIH04778.1; -; Genomic_DNA.
DR   RefSeq; WP_038061980.1; NZ_JQLF01000014.1.
DR   AlphaFoldDB; A0A075WW98; -.
DR   STRING; 289377.HL41_09065; -.
DR   PaxDb; 289377-HL41_09065; -.
DR   KEGG; tcm:HL41_09065; -.
DR   eggNOG; COG1220; Bacteria.
DR   HOGENOM; CLU_033123_0_0_0; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000028481; 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:AIH04778.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:AIH04778.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028481}.
FT   DOMAIN          52..331
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          334..428
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         63..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         392
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   442 AA;  50639 MW;  B921B3E1DC0D02F4 CRC64;
     MNEPKEFTPR EIVAELNRYI VGQDRAKKAV AIAMRNRWRR QQLKEDLKEE IYPKNILMIG
     PTGVGKTEIA RRLAKLSNAP FLKVEATKFT EVGYVGRDVE SMIRDLVHIA VKMVREEEEK
     KVLEKAKTLA EERLVDLLIP PISSKVEYDP LTREKFLKML RDGVLNDRYV EIEVEASQKP
     PTIEIFAASG LEEIEMQLRD MLSTILPFKP KKRKVKVKEA LEILTKEEAA KLIDMDKVIK
     EAIRRTETNG IIFIDEIDKI ASRGEGHGPD VSREGVQRDL LPIVEGTTVN TKYGMVRTDY
     ILFIGSGAFH IAKPSDLIPE LQGRFPIRVE LDPLTKEDFI RILTETENAI IKQYKALLAT
     EQVEIDFTPE AIEEIAKVAF ELNQKMENIG ARRLYTVMEK VLEDISFEAP DIAPTRVVIT
     PEYVREKLEN IIQDQELAKF IL
//
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