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Database: UniProt
Entry: A0A0J9BC17_9GAMM
LinkDB: A0A0J9BC17_9GAMM
Original site: A0A0J9BC17_9GAMM 
ID   A0A0J9BC17_9GAMM        Unreviewed;       444 AA.
AC   A0A0J9BC17;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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:KMV70709.1};
GN   ORFNames=AI29_10385 {ECO:0000313|EMBL:KMV70709.1};
OS   bacteria symbiont BFo2 of Frankliniella occidentalis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales.
OX   NCBI_TaxID=1628856 {ECO:0000313|EMBL:KMV70709.1, ECO:0000313|Proteomes:UP000036794};
RN   [1] {ECO:0000313|EMBL:KMV70709.1, ECO:0000313|Proteomes:UP000036794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFo2 {ECO:0000313|EMBL:KMV70709.1,
RC   ECO:0000313|Proteomes:UP000036794};
RA   Facey P.D., Hitchings M.D., Hegarty M.J., Pachebat J.A., Morgan L.V.,
RA   Hoeppner J.E., Whitten M.A., Dyson P.J., Del Sol R.;
RT   "The draft genomes, genome evolution and classification of BFo1 and BFo2
RT   two insect symbionts isolated from Western Flower Thrips (Frankliniella
RT   occidentalis [Pergande]).";
RL   Submitted (MAY-2014) 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:KMV70709.1}.
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DR   EMBL; JMSP01000321; KMV70709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J9BC17; -.
DR   SMR; A0A0J9BC17; -.
DR   STRING; 1628856.WB67_05570; -.
DR   PATRIC; fig|1628856.3.peg.2081; -.
DR   Proteomes; UP000036794; 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; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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, ECO:0000313|EMBL:KMV70709.1};
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:KMV70709.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:KMV70709.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036794}.
FT   DOMAIN          49..333
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          336..432
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   REGION          139..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         322
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         394
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   444 AA;  49802 MW;  CA20F09DA527EBA7 CRC64;
     MSEMTPREIV SELNRFIIGQ DNAKRAVSIA LRNRWRRMQL NDELRHEVTP KNILMIGPTG
     VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTEAAVKM VRSQAIEKNK
     ARAVEHAEDR ILDVLIPPAK NNWGQSESSQ EESSTRQSFR KKLREGQLDD KEIEIDLAAS
     PMDVEIMAPP GMEEMTNQLQ SMFQNMGNQK QKSRKLKIKD AMKLLIEEEA ARLVNPEELK
     QQAIEAVEQH GIVFIDEIDK ICKRGGQSSG PDVSREGVQR DLLPLVEGCT VSTKHGTVKT
     DHILFIASGA FQVASPSDLI PELQGRLPIR VELQALTVND FERILTEPTA SVTVQYKALM
     ETEGVNIDFT DDGIRRIAEA AWQVNETTEN IGARRLYTVL EKLVEDISFE ASDRSGETVT
     IDADYVSKHL DVLVADEDLS RFIL
//
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