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Database: UniProt
Entry: A0A0H2LWX1_VARPD
LinkDB: A0A0H2LWX1_VARPD
Original site: A0A0H2LWX1_VARPD 
ID   A0A0H2LWX1_VARPD        Unreviewed;       442 AA.
AC   A0A0H2LWX1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, 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   ECO:0000313|EMBL:KLN54226.1};
GN   ORFNames=VPARA_45750 {ECO:0000313|EMBL:KLN54226.1};
OS   Variovorax paradoxus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN54226.1, ECO:0000313|Proteomes:UP000035170};
RN   [1] {ECO:0000313|EMBL:KLN54226.1, ECO:0000313|Proteomes:UP000035170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBEA6 {ECO:0000313|EMBL:KLN54226.1,
RC   ECO:0000313|Proteomes:UP000035170};
RA   Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA   Daniel R.;
RT   "Genome sequence of Variovorax paradoxus TBEA6.";
RL   Submitted (MAR-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:KLN54226.1}.
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DR   EMBL; JZWI01000025; KLN54226.1; -; Genomic_DNA.
DR   RefSeq; WP_047786123.1; NZ_JZWI01000025.1.
DR   AlphaFoldDB; A0A0H2LWX1; -.
DR   PATRIC; fig|34073.19.peg.4678; -.
DR   Proteomes; UP000035170; 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};
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:KLN54226.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:KLN54226.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035170}.
FT   DOMAIN          48..335
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          334..430
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         59..64
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;  48989 MW;  A9342BA8F1B6926E CRC64;
     MSMTPQEIVS ELDNHIVGQP GAKRAVAIAL RNRWRRQQVE EKLRAEITPK NILMIGPTGV
     GKTEIARRLA RLADAPFIKV EATKFTEVGY VGKDVDSIIR DLAEIAVKQT RESESAKVRA
     RAEDAAEDRI LDVLLPPARG ADGATPALDG PNPTRQAFRK KLREHQLDDK EIELDLAETR
     APLEIMGPAG MEEMTEQLRG MFGQLGGGKR KTRKLKIAEA LRLLIDEEAA KLVNEDEIRT
     QAITNAEQNG IVFIDEIDKV ATRSEAQGSD VSRQGVQRDL LPLVEGTAVS TKYGVVRTDH
     ILFIASGAFH LSKPSDLIPE MQGRFPIRVE LQPLSVSDFE SILTQTRASL VKQYQALLAT
     EGVTLEFTPE GVTRLASIAF EVNERTENIG ARRLSTVMER LLDEVSFDAT RIEGQTIRID
     AAYVDERLAA LSHDEDLSRF IL
//
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