GenomeNet

Database: UniProt
Entry: A0A2V1K140_9BURK
LinkDB: A0A2V1K140_9BURK
Original site: A0A2V1K140_9BURK 
ID   A0A2V1K140_9BURK        Unreviewed;       866 AA.
AC   A0A2V1K140;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:PWF24158.1};
GN   ORFNames=DD235_07650 {ECO:0000313|EMBL:PWF24158.1};
OS   Corticimicrobacter populi.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Corticimicrobacter.
OX   NCBI_TaxID=2175229 {ECO:0000313|EMBL:PWF24158.1, ECO:0000313|Proteomes:UP000245212};
RN   [1] {ECO:0000313|Proteomes:UP000245212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3d-2-2 {ECO:0000313|Proteomes:UP000245212};
RA   Li Y.;
RL   Submitted (MAY-2018) 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   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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:PWF24158.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QETA01000002; PWF24158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1K140; -.
DR   Proteomes; UP000245212; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
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; TIGR03346; chaperone_ClpB; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245212};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   866 AA;  96131 MW;  BC692EDE9ECDE124 CRC64;
     MRFDRFTTKF QQALADAQSL AVRNDHPYIE PVHVLSALLA DTDSGAGSLL ARAGVAVNRV
     GAALDGALKA LPQVQGGDGN VQVGRDLQAV LARTDKEAAK RGDTYIASEL FLLALADDKG
     EAGRILRDAG LQRAPLEAAI EAVRGGASVQ DAEGEANREA LGKYTLDLTA RAREGKLDPV
     IGRDDEIRRA IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNNEVPE TLKNKRVLSL
     DLAALLAGAK FRGEFEERLK SVLKELAQEA GNCIVFIDEI HTMVGAGKAE GAMDAGNMLK
     PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVLVGE PDVESTIAIL RGLQERYELH
     HGVQITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAAAR IRMEIDSKPE VMDRLDRRII
     QLKIEREAVR KETDEASLRR LKAIEDELES LQREYNDYEE IWKAEKAAVQ GTQAIKEEIE
     RLRAEMAEAQ RKGQFDKLAE LQYGQLPELE ARLRTAEGSE KAASEGGSER PRLLRTQVGT
     EEIAEVVSRA TGIPVAKMMQ GERTKLLEME SFLHKRVVGQ DEAVRLVSDA IRRSRSGLSD
     PNRPYGSFLF LGPTGVGKTE LTKALAEFLF DAEDHLIRID MSEFMEKHSV ARLIGAPPGY
     VGYEEGGYLT EAVRRKPYSV VLLDEVEKAH PDVFNVLLQV LDDGRLTDGQ GRTVDFRNTV
     IVMTSNLGSQ QIQSMANQPY EAVKAVVWDE LKQAFRPEFL NRIDEVVVFH ALDSKNIESI
     ARIQLQRLAQ RLQKMDMELD VSEAALAQIA KAGFDPVFGA RPLKRAIQQH IENPVARLIL
     EGRFGPRDVV PVDWRDEQFV FSRVLQ
//
DBGET integrated database retrieval system