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Database: UniProt
Entry: A0A0U3LI14_9BURK
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Original site: A0A0U3LI14_9BURK 
ID   A0A0U3LI14_9BURK        Unreviewed;       772 AA.
AC   A0A0U3LI14;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding protein {ECO:0000313|EMBL:ALV07727.1};
GN   ORFNames=RD2015_3269 {ECO:0000313|EMBL:ALV07727.1};
OS   Roseateles depolymerans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=76731 {ECO:0000313|EMBL:ALV07727.1, ECO:0000313|Proteomes:UP000060699};
RN   [1] {ECO:0000313|EMBL:ALV07727.1, ECO:0000313|Proteomes:UP000060699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42856 {ECO:0000313|EMBL:ALV07727.1,
RC   ECO:0000313|Proteomes:UP000060699};
RA   Kim K.M.;
RT   "Complete genome of Roseateles depolymerans KCTC 42856.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK.
CC       {ECO:0000256|ARBA:ARBA00025613}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP013729; ALV07727.1; -; Genomic_DNA.
DR   RefSeq; WP_058935791.1; NZ_QUMT01000001.1.
DR   AlphaFoldDB; A0A0U3LI14; -.
DR   STRING; 76731.RD2015_3269; -.
DR   KEGG; rdp:RD2015_3269; -.
DR   PATRIC; fig|76731.3.peg.3349; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000060699; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043335; P:protein unfolding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR013461; ClpA.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR02639; ClpA; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Hydrolase {ECO:0000313|EMBL:ALV07727.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ALV07727.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060699};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          142..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   772 AA;  84419 MW;  B3B6CAA34E8A13C4 CRC64;
     MIAQELEVSL HMAFVEARQQ RHEFITVEHL LMALLDNPSA AEVLRACAAN IEDLRKSLAQ
     FIKENTPTVG GTDEVDTQPT LGFQRVIQRA IMHVQSTGNG KKEVTGANVL VAIFGEKDSH
     AVYYLHQQGV TRLDVVNYIA HGIKKSEPPE PPKGPEGSGN ESEREEGDAQ GGSGKGSPLE
     QFTQNLNQQA RDGKIDPLIG RELEVERVVQ VLCRRRKNNP LLVGEAGVGK TAIAEGLAWR
     ITEGQVPDVL AEAVVYSLDM GALLAGTKYR GDFEQRLKAV IKQLKDQPGA ILFIDEIHTL
     IGAGAASGGT LDASNLLKPA LSSGQLKCIG ATTFSEYRGI FEKDAALSRR FQKIDVVEPS
     VEQTVEILKG LKSRFEEHHS VKYALGALQA AAELSAKYIN DRHLPDKAID VIDEAGAAQR
     VLPKSKQKKT ITRAEVEDIV AKIARIPPAS VSSDDRGKLK SLDRDLKSVV FGQDPAIDAL
     AAAIKMARSG LGKPDKPIGS FLFTGPTGVG KTEVAKQLAY ILGIELIRFD MSEYMERHAV
     SRLIGAPPGY VGFDQGGLLT EAVTKKPHAV LLLDEIEKAH PDVFNVLLQV MDHGTLTDNN
     GRKADFRNVI IIMTTNAGAE ALQKATIGFT TKREQGDEMG DIKRLFTPEF RNRLDAIVHF
     RSLDEDIILR VVDKFLLQLE SQLQEKKVEV TFSDALRKHL AAKGFDPQMG ARPMQRLIQD
     TIRRALADEL LFGKLVDGGR LNVDVDDKGE VQLDITPTKK DNKPKAEPAT AD
//
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