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Database: UniProt
Entry: A0A2P8KL42_9BURK
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ID   A0A2P8KL42_9BURK        Unreviewed;       873 AA.
AC   A0A2P8KL42;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
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:PSL83698.1};
GN   ORFNames=C7T35_15035 {ECO:0000313|EMBL:PSL83698.1}, GXN78_04415
GN   {ECO:0000313|EMBL:NDZ12123.1};
OS   Variovorax sp. WS11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1105204 {ECO:0000313|EMBL:PSL83698.1, ECO:0000313|Proteomes:UP000241151};
RN   [1] {ECO:0000313|EMBL:PSL83698.1, ECO:0000313|Proteomes:UP000241151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WS11 {ECO:0000313|EMBL:PSL83698.1,
RC   ECO:0000313|Proteomes:UP000241151};
RA   Crombie A.T., Mejia-Florez N.L., Murrell C.;
RT   "Isoprene degraders from the Poplar phyllosphere.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:NDZ12123.1, ECO:0000313|Proteomes:UP000479786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WS11 {ECO:0000313|EMBL:NDZ12123.1,
RC   ECO:0000313|Proteomes:UP000479786};
RA   Dawson R.A., Larke-Mejia N.L., Crombie A.T., Ul-Haque M.F., Murrell J.C.;
RT   "Isoprene oxidation by the Gram negative model bacterium Variovorax sp.
RT   WS11.";
RL   Submitted (FEB-2020) 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:PSL83698.1}.
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DR   EMBL; JAAGOW010000001; NDZ12123.1; -; Genomic_DNA.
DR   EMBL; PXZZ01000018; PSL83698.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8KL42; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000241151; Unassembled WGS sequence.
DR   Proteomes; UP000479786; 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 78, MITOCHONDRIAL; 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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          410..459
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   873 AA;  95938 MW;  AC5E45F19F309ED8 CRC64;
     MRQDKLTTKF QEALADAQSL ALGNDNAYIE PIHLLVAMLR QDDGPRALLE RAGANVPGLL
     NAAEAAIKKL PQVSGHDQVQ VGPDLGKLLQ ATEKEAIKRN DQFIAGELFL LALADSKAEI
     GNLARSHGVT RKSVEAAIDA VRGGQGVNSA DAEGQREALK KYTLDLTERA RLGKLDPVIG
     RDEEIRRAIQ VLQRRTKNNP VLIGEPGVGK TAIVEGLAQR IVAGEVPESL KGKRVLSLDM
     AALLAGAKYR GEFEERLKTV LHELAKDEGQ TIVFIDELHT MVGAGKAEGA MDAGNMLKPA
     LARGELHCVG ATTLDEYRKY IEKDAALERR FQKILVGEPS VEATVAILRG LKEKYEVHHG
     VDITDPAIVA AAELSDRYVT DRFLPDKAID LIDEAAARIK IEMDSKPEVM DRLDRRLIQL
     QIEREAVRRE KDEASQKRLG LIEDDIKRVQ KELADLDEIW QAEKAQAQGS AQIREEIDKI
     KFQIAEFTSK GDFNKVAELQ YGKLPGLEKR LKEAQDTEAN KGKSSAPTLL RTQVGAEEIA
     EVVARATGIP VSKLMQGERD KLLQMEAKLH ERVVGQDEAI GAVANAIRRS RSGLADPNRP
     TGSFLFLGPT GVGKTELCKA LAGFLFDSED HLIRVDMSEF MEKHSVARLI GAPPGYVGYE
     EGGHLTEAVR RKPYSVLLLD EVEKAHPDVF NVLLQVLDDG RLTDGQGRTV NFKNTVIVMT
     SNIGSPIIQA MVGRPAEEIK DAVWDELKNY FRPEFLNRID ETVVFHALDA RNIEAIAAIQ
     LRVLQERLAK MDLALEVSPA ALAEIAKVGF DPVFGARPLK RAIQHRIENP LSKLLLDGSF
     GPKDTIVVTT DPIRTPGQFE FHKAGEPRAE AVA
//
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