ID A0A4Q3LHW8_9BURK Unreviewed; 874 AA.
AC A0A4Q3LHW8;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
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:RYF16410.1};
GN ORFNames=EOO30_11200 {ECO:0000313|EMBL:RYF16410.1};
OS Comamonadaceae bacterium.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1871071 {ECO:0000313|EMBL:RYF16410.1, ECO:0000313|Proteomes:UP000292155};
RN [1] {ECO:0000313|EMBL:RYF16410.1, ECO:0000313|Proteomes:UP000292155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PMG_248 {ECO:0000313|EMBL:RYF16410.1};
RX PubMed=30498029; DOI=.1073/pnas.1812668115;
RA Crombie A.T., Larke-Mejia N.L., Emery H., Dawson R., Pratscher J.,
RA Murphy G.P., McGenity T.J., Murrell J.C.;
RT "Poplar phyllosphere harbors disparate isoprene-degrading bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:13081-13086(2018).
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:RYF16410.1}.
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DR EMBL; SEAY01000045; RYF16410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q3LHW8; -.
DR Proteomes; UP000292155; 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:UP000292155};
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..490
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 874 AA; 96801 MW; B7F432479FCF8814 CRC64;
MRIDKLTTKF QEALGEAQSL ALANDHAYIE PPHLLVAMLR QEDGPRALLQ RAGVNVPGLL
AAAEGAMHKL PQVQGQEQIG VGRDLAVLLQ GAEKEALKRN DQFIASENFL LALAETKQDI
GRIARENGLS RKALEAAVDA VRGGQNVNSA ESEGQREALK KYTLDLTERA RMGKLDPVIG
RDEEIRRAIQ VLQRRTKNNP VLIGEPGVGK TAIVEGLAQR IIAGEVPETL KGKRVLSLDM
AALLAGAKYR GEFEERLKSV LTELAKDEGQ TIVFIDELHT MVGAGKAEGA MDAGNMLKPA
LARGELHCVG ATTLDEYRKY IEKDAALERR FQKILVGEPT VEATIAILRG LQEKYEVHHG
VEITDPAIVA AAELSHRYIT DRFLPDKAID LIDEAASKVK IEIDSKPEAI DRLDRRMIQL
QIEREAVKKE KDEASQKRLG LIEEEIARLR QEISDLEEIW KSEKAQAQGS AHVKEEIDKL
RREIEESTRK GDFNKVAELQ YGKLPTLEKQ LKEAQAAETA KGKSGKPQLL RTQVGADEIA
EVVARATGIP VSKLMQGERE KLLLMEDKLH ERVVGQDEAI SAVANAIRRS RSGLSDPNRP
TGSFLFLGPT GVGKTELCKA LAGFLFDSEE HLIRVDMSEF MEKHSVARLI GAPPGYVGYE
EGGYLTEAVR RKPYSVILLD EVEKAHHDVF NVLLQVLDDG RLTDGQGRTV DFKNAVIVMT
SNIGSHMIQA MVGKPYEDVK EAVWDELKNH FRPEFLNRID ETVVFHGLGA DHIARIAKIQ
LRVLEQRMAK MDLQLEVTPA ALEELAKVGF DPVFGARPLK RAIQQRIENP LSRLILEGRF
PPKSQVQVEV DPVREPGVFH FKGAVEPAPE SMSA
//