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Database: UniProt
Entry: K2KLU0_9PROT
LinkDB: K2KLU0_9PROT
Original site: K2KLU0_9PROT 
ID   K2KLU0_9PROT            Unreviewed;       436 AA.
AC   K2KLU0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=P24_02631 {ECO:0000313|EMBL:EKE78420.1};
OS   Oceanibaculum indicum P24.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassobaculaceae; Oceanibaculum.
OX   NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE78420.1, ECO:0000313|Proteomes:UP000006746};
RN   [1] {ECO:0000313|EMBL:EKE78420.1, ECO:0000313|Proteomes:UP000006746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P24 {ECO:0000313|EMBL:EKE78420.1,
RC   ECO:0000313|Proteomes:UP000006746};
RX   PubMed=23209207; DOI=10.1128/JB.01859-12;
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of Oceanibaculum indicum Type Strain P24.";
RL   J. Bacteriol. 194:6942-6942(2012).
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:EKE78420.1}.
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DR   EMBL; AMRL01000002; EKE78420.1; -; Genomic_DNA.
DR   RefSeq; WP_008943143.1; NZ_AMRL01000002.1.
DR   AlphaFoldDB; K2KLU0; -.
DR   STRING; 1207063.P24_02631; -.
DR   PATRIC; fig|1207063.3.peg.533; -.
DR   eggNOG; COG1220; Bacteria.
DR   Proteomes; UP000006746; 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; IPR001270; ClpA/B.
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   PRINTS; PR00300; CLPPROTEASEA.
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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   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:EKE78420.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00249}; Protease {ECO:0000313|EMBL:EKE78420.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006746}.
FT   DOMAIN          49..325
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          328..417
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         249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         314
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
FT   BINDING         386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00249"
SQ   SEQUENCE   436 AA;  48410 MW;  256D057ED819CB45 CRC64;
     MTAFSPREIV SELDRYIVGQ KDAKRAVAIA LRNRWRRQQL PEHLREEVLP KNILMIGPTG
     VGKTEIARRL AKLAQAPFMK VEATKFTEVG YVGRDVEQII RDLVEIALTQ TRERLRQEVQ
     AKAELAAEER VITALVGEGA AADTRHRFRK MLREGQLDSR EIEVEVADNA GASMPTMDIP
     GMPGAQMGMI NLNDIFGKAF GQRTRKKKLS VADSYAVLTE EEADKLLDEE AVTREAIQSV
     EQNGIVFLDE IDKICARSER SGADVSREGV QRDLLPLIEG TTVATKRGPV KTDHILFIAS
     GAFHLAKPSD LLPELQGRLP IRVELQALTR DDFKRILTEP EASLIKQYVA LLATEQVTLD
     FREDAIDALA TLSAEVNASV ENIGARRLHT VMERLLEEVS FTATDKPGET ITVDAAFVQK
     HVGDLAKNAD LSKFIL
//
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