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Database: UniProt
Entry: A0A2M6VQI3_9BURK
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ID   A0A2M6VQI3_9BURK        Unreviewed;       867 AA.
AC   A0A2M6VQI3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=B9Z41_01455 {ECO:0000313|EMBL:PIT80616.1};
OS   Limnohabitans sp. JirII-31.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Limnohabitans.
OX   NCBI_TaxID=1977908 {ECO:0000313|EMBL:PIT80616.1, ECO:0000313|Proteomes:UP000228925};
RN   [1] {ECO:0000313|EMBL:PIT80616.1, ECO:0000313|Proteomes:UP000228925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JirII-31 {ECO:0000313|EMBL:PIT80616.1,
RC   ECO:0000313|Proteomes:UP000228925};
RA   Kasalicky V., Mehrshad M., Andrei S.-A., Salcher M., Kratochvilova H.,
RA   Simek K., Ghai R.;
RT   "Unexpected and diverse lifestyles within the genus Limnohabitans.";
RL   Submitted (APR-2017) 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:PIT80616.1}.
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DR   EMBL; NESA01000001; PIT80616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M6VQI3; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000228925; 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:UP000228925};
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   867 AA;  95673 MW;  267A78E1AACDCFD9 CRC64;
     MRLDKLTTKF QEALSEAQTL ALGNDHAYIE PSHVVVAMLR QDDGPKSLLQ RAGANVTGLA
     AAAETAMNRL PKVQGQEQVQ VGRDLVSLIQ AAEKESIKRG DQYIASELFL LALCDNKGDW
     GKLARDNGLT RQSLEAAVTA VRGGQKVDNA ESEGQRESLK KYCVDLTERA RSGKLDPVIG
     RDDEIRRAIQ VLQRRTKNNP VLIGEPGVGK TAIVEGLAQR IVSGEVPDSL KGKRVLSLDM
     AALLAGAKYR GEFEERLKSV LTELAKDEGQ TIVFIDELHT MVGAGKAEGA MDAGNMLKPA
     LARGELHCVG ATTLDEYRKY IEKDAALERR FQKIIVGEPT VEATIAILRG LQEKYEVHHG
     VEITDPAIVA AAELSHRYIT DRFLPDKAID LIDEAAAKIK IEIDSKPEVM DKLDRRLIQL
     KIEREAVRKE KDEASQKRLG LLEEEITKLG KDYADLEEIW KSEKASAHGG AQVKEEIDRI
     RFQIEEFTRK GDFNKVAELQ YGKLPELEKR LKEANAKESS KTAKPGTHRL LRTQVGAEEI
     AEVVARATGI PVSKLMQGER DKLLQMEDKL HQRVVGQEEA ITAVANAIRR SRAGLGDPNR
     PTGSFLFLGP TGVGKTELCK ALAGFLFDSE DHMIRIDMSE FMEKHSVSRL IGAPPGYVGY
     DEGGYLTEAV RRKPYSVLLL DEVEKAHPDV FNILLQVLDD GRLTDGQGRT VDFKNTVIVM
     TSNIGSPIIQ SMVGQDPQDI KDAVWDELKS HFRPEFLNRI DETVVFHSLD AQHIARIADI
     QLKVLSERLA KMDLGLQVSP AALAELAKVG FDPVFGARPL KRAIQQRIEN PLSKLLLEGK
     FGPKDAIAVS VDPVRAPGEF AFTKVAA
//
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