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Database: UniProt
Entry: A0A4Q3LHW8_9BURK
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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
//
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