ID A0A0U5LJ82_9GAMM Unreviewed; 444 AA.
AC A0A0U5LJ82;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:CUU22348.1};
GN ORFNames=EM595_0111 {ECO:0000313|EMBL:CUU22348.1};
OS Duffyella gerundensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Duffyella.
OX NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU22348.1, ECO:0000313|Proteomes:UP000059419};
RN [1] {ECO:0000313|Proteomes:UP000059419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Blom J.;
RL Submitted (NOV-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}.
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DR EMBL; LN907827; CUU22348.1; -; Genomic_DNA.
DR RefSeq; WP_067426733.1; NZ_LN907827.1.
DR AlphaFoldDB; A0A0U5LJ82; -.
DR STRING; 1619313.EM595_0111; -.
DR GeneID; 84614896; -.
DR KEGG; ege:EM595_0111; -.
DR PATRIC; fig|1619313.3.peg.113; -.
DR OrthoDB; 9804062at2; -.
DR Proteomes; UP000059419; Chromosome 1.
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:CUU22348.1};
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:CUU22348.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW Protease {ECO:0000313|EMBL:CUU22348.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059419}.
FT DOMAIN 49..333
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 336..430
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 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; 49559 MW; 58541859B6A119DD CRC64;
MSEMTPREIV SELNRFIIGQ DGAKRAVAIA LRNRWRRMQL DEELRHEVTP KNILMIGPTG
VGKTEIARRL AKLAHAPFIK VEATKFTEVG YVGKEVDSII RDLTDAAIKM VRMQAIEKNK
YRAEEMAEER ILDALIPPAK NNWGQPEASA EPSAARQSFR KKLREGQLDD KEIEINLAAA
PMGVEIMSPP GMEEMTSQLQ SMFQNLGGQK QNARKLKIKE AMKLLIEEEA AKLVNPEELK
QEAIDAVEQH GIVFVDEIDK ICKRGGQSSG PDVSREGVQR DLLPLVEGCT VSTKHGMVKT
DHILFIASGA FQVASPSDLI PELQGRLPIR VELQALTVND FERILTEPNA SVTVQYKALM
ATEGVNIDFT DDGIRRIAEA AWQVNETTEN IGARRLHTVL ERLMEEISYN ASDRSGDSVT
IDAEYVGKHL DQLVADEDLS RFIL
//
