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Database: UniProt
Entry: A0A2Z4FNE8_9DELT
LinkDB: A0A2Z4FNE8_9DELT
Original site: A0A2Z4FNE8_9DELT 
ID   A0A2Z4FNE8_9DELT        Unreviewed;       465 AA.
AC   A0A2Z4FNE8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=DN745_13585 {ECO:0000313|EMBL:AWV90305.1};
OS   Bradymonas sediminis.
OC   Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae; Bradymonas.
OX   NCBI_TaxID=1548548 {ECO:0000313|EMBL:AWV90305.1, ECO:0000313|Proteomes:UP000249799};
RN   [1] {ECO:0000313|EMBL:AWV90305.1, ECO:0000313|Proteomes:UP000249799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FA350 {ECO:0000313|EMBL:AWV90305.1,
RC   ECO:0000313|Proteomes:UP000249799};
RA   Guo L.-Y., Li C.-M., Wang S., Du Z.-J.;
RT   "Lujinxingia sediminis gen. nov. sp. nov., a new facultative anaerobic
RT   member of the class Deltaproteobacteria, and proposal of Lujinxingaceae
RT   fam. nov.";
RL   Submitted (JUN-2018) 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}.
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DR   EMBL; CP030032; AWV90305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z4FNE8; -.
DR   KEGG; bsed:DN745_13585; -.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000249799; 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:InterPro.
DR   GO; GO:0036402; F:proteasome-activating activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043335; P:protein unfolding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
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   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249799}.
FT   DOMAIN          54..354
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          357..451
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   BINDING         23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         65..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   465 AA;  52762 MW;  99AEF0147D89EA74 CRC64;
     MEFDREQDLT PREIVAELDR FIVGQRAAKR AVAVALRNRW RRQQVGDELR DEIMPKNIIM
     IGPTGVGKTE IARRLARLAR APFLKVEASK FTEVGYVGRD VESMVRDLLD LGINLVKAEA
     EAKVELRARE AAEDRILEQL KGRAAPRRPL DERDEDRKTF IAGVDGVMQS DEGPLDEREL
     LRRRLRDGEL DQEYVEVDVA ETHNPMADMF SKQPGMEQMN LGGVLGNIFP ERRKQKRVKV
     GEAMRLLINE ESSRLIDMDH VISEALERTT QGGIIFLDEL DKIAGRESSS GPDVSREGVQ
     RDLLPIVEGS SVSTKHGIVK TDHILFIAAG AFHVSKPSDL IPELQGRFPI RVELTSLTQQ
     DFRRILTEPQ NSLTRQYTAL LKPEGLEIGF DDEAIDTIAE MAFRVNNNLE NIGARRLHTI
     MEQVFEELAF EAPDMEDMNV QITADYVREK LEGILENEDL SRYIL
//
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