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Database: UniProt
Entry: A0A0J8GQR5_9ALTE
LinkDB: A0A0J8GQR5_9ALTE
Original site: A0A0J8GQR5_9ALTE 
ID   A0A0J8GQR5_9ALTE        Unreviewed;       444 AA.
AC   A0A0J8GQR5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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:KMT65057.1};
GN   ORFNames=XM47_11345 {ECO:0000313|EMBL:KMT65057.1};
OS   Catenovulum maritimum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Catenovulum.
OX   NCBI_TaxID=1513271 {ECO:0000313|EMBL:KMT65057.1, ECO:0000313|Proteomes:UP000037600};
RN   [1] {ECO:0000313|EMBL:KMT65057.1, ECO:0000313|Proteomes:UP000037600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1 {ECO:0000313|EMBL:KMT65057.1,
RC   ECO:0000313|Proteomes:UP000037600};
RA   Li Y., Li D., Chen G., Du Z.;
RT   "Draft Genome Sequence of the Novel Agar-Digesting Marine Bacterium Q1.";
RL   Submitted (APR-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}.
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:KMT65057.1}.
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DR   EMBL; LAZL01000016; KMT65057.1; -; Genomic_DNA.
DR   RefSeq; WP_048692564.1; NZ_KQ130491.1.
DR   AlphaFoldDB; A0A0J8GQR5; -.
DR   STRING; 1513271.XM47_11345; -.
DR   PATRIC; fig|1513271.3.peg.2309; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000037600; 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   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:KMT65057.1};
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:KMT65057.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:KMT65057.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037600}.
FT   DOMAIN          49..333
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          336..435
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         257
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;  49725 MW;  8B222AA9F71CFB90 CRC64;
     MSEMTPKEIV HELNSHIIGQ DKAKRAVAIA LRNRWRRMQL DPDLRQEVTP KNILMIGPTG
     VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVETII RDLADISIKM TREQATVKVK
     HRAEEAAEER ILDALLPKPQ AMFGEEEPQD TGSNTRQIFR KKLREGTLDD KEIEIDVAAP
     QVGVEIMAPP GMEEMTNQLQ GMFQNLSGNS AKKTRKMKVK EAYKLLVEEE AGRLVNQEEL
     KEQAIETLEQ NGIVFIDEID KICKRGESSG PDVSREGVQR DLLPLVEGST VTTKHGMVKT
     DHILFIASGA FQMAKPSDLI PELQGRLPIR VELEALTAHD FVRILTEPNA SLTEQYKALM
     ATEGVSVDFS QDGIEKIANA AFRVNEKTEN IGARRLHTVM EKLMEEVSYD ASEMSGQSIT
     VDADYVSKFL NDLVEDEDLS RFIL
//
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