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Entry: A0A085FZC8_9ENTR
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ID   A0A085FZC8_9ENTR        Unreviewed;       444 AA.
AC   A0A085FZC8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, 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:KFC76823.1};
GN   ORFNames=GBAG_4281 {ECO:0000313|EMBL:KFC76823.1};
OS   Buttiauxella agrestis ATCC 33320.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Buttiauxella.
OX   NCBI_TaxID=1006004 {ECO:0000313|EMBL:KFC76823.1, ECO:0000313|Proteomes:UP000028653};
RN   [1] {ECO:0000313|EMBL:KFC76823.1, ECO:0000313|Proteomes:UP000028653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33320 {ECO:0000313|EMBL:KFC76823.1,
RC   ECO:0000313|Proteomes:UP000028653};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
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:KFC76823.1}.
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DR   EMBL; JMPI01000074; KFC76823.1; -; Genomic_DNA.
DR   RefSeq; WP_034461420.1; NZ_JMPI01000074.1.
DR   AlphaFoldDB; A0A085FZC8; -.
DR   STRING; 1006004.GBAG_4281; -.
DR   eggNOG; COG1220; Bacteria.
DR   OrthoDB; 9804062at2; -.
DR   Proteomes; UP000028653; 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:KFC76823.1};
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:KFC76823.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00249};
KW   Protease {ECO:0000313|EMBL:KFC76823.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028653}.
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         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;  49736 MW;  B1282FDF231695C0 CRC64;
     MSEMTPREIV SELNKHIIGQ DNAKRSVAIA LRNRWRRMQL DEELRHEVTP KNILMIGPTG
     VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII RDLTDSAMKM VRLQSIEKNR
     YRAEEMAEER ILDVLIPPAK NNWGQNETAP EPSAARQSFR KKLREGQLDD KEIEIDLAAA
     PMGVEIMAPP GMEEMTSQLQ SMFQNLGGQK QKPRKLKIKD AMKLLIEEEA AKLVNPEELK
     QDAIDAVEQH GIVFIDEIDK ICKRGGNSSG PDVSREGVQR DLLPLVEGCT VSTKHGMVKT
     DHILFIASGA FQVASPSDLI PELQGRLPIR VELQALTVED FERILTEPNA SITVQYKALL
     GTEGVNIDFT EDGIRRIAQA AWQVNESTEN IGARRLHTVL ERLVEDISYD ASEMNGQSIL
     IDGEYVSKHL DELVADEDLS RFIL
//
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