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Database: UniProt
Entry: A0A2N3IAA0_9BACT
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ID   A0A2N3IAA0_9BACT        Unreviewed;       455 AA.
AC   A0A2N3IAA0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=Rain11_2108 {ECO:0000313|EMBL:PKQ67246.1};
OS   Raineya orbicola.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Raineyaceae; Raineya.
OX   NCBI_TaxID=2016530 {ECO:0000313|EMBL:PKQ67246.1, ECO:0000313|Proteomes:UP000233387};
RN   [1] {ECO:0000313|EMBL:PKQ67246.1, ECO:0000313|Proteomes:UP000233387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPSPC-11 {ECO:0000313|EMBL:PKQ67246.1,
RC   ECO:0000313|Proteomes:UP000233387};
RA   Albuquerque L., Polonia A.R.M., Barroso C., Froufe H.J.C., Lage O.,
RA   Lobo-Da-Cunha A., Egas C., Da Costa M.S.;
RT   "Raineya orbicola gen. nov., sp. nov. a slightly thermophilic bacterium of
RT   the phylum Bacteroidetes and the description of Raineyaceae fam. nov.";
RL   Submitted (JUN-2017) 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}.
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:PKQ67246.1}.
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DR   EMBL; NKXO01000036; PKQ67246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3IAA0; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000233387; 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: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:PKQ67246.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:PKQ67246.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233387}.
FT   DOMAIN          51..342
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          345..446
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         62..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         266
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         403
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   455 AA;  51356 MW;  4D3A67E396B7A787 CRC64;
     MNREHLTPQQ IVTELDKYII GQKEAKKNVA IALRNRWRRM NSPAEIQNEI IPNNILMIGS
     TGVGKTEIAR RLAKLADAPF VKVEASKFTE VGYVGRDVES MVRDLVEQAV GMVKQQKQEE
     VKQKAIEAVE EIILDALIPP VRKPISEGVG FNLEKNDEVE LNERTRERFR EKIRNGELDH
     RKIEIDIKQT ISNVGVLGSG IDEVSMMNLQ EMLSNFMPTK TKKRKVTIAE AKKILLEEET
     SKMIDMDEVK EEAIRRAENA GIIFIDEIDK IASSGSKQGP DVSREGVQRD LLPIVEGSSV
     NTKYGVVKTD HILFIAAGAF HVSKPSDLIP ELQGRFPIRV ELQALTKDDF YHILKEPRNA
     LTKQYEALLM AEGVELDFED EALEKIAEIA FQINSEVENI GARRLQTVMS ALLNDFLFEI
     PDTIQPPAKI IVTASMVSEK LNHLVKNKDL SHYIL
//
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