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Database: UniProt
Entry: A0A0Q5VAD1_9CAUL
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Original site: A0A0Q5VAD1_9CAUL 
ID   A0A0Q5VAD1_9CAUL        Unreviewed;       862 AA.
AC   A0A0Q5VAD1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=ASG17_01645 {ECO:0000313|EMBL:KQS57452.1};
OS   Brevundimonas sp. Leaf363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS57452.1, ECO:0000313|Proteomes:UP000051182};
RN   [1] {ECO:0000313|EMBL:KQS57452.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS57452.1,
RC   ECO:0000313|Proteomes:UP000051182};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS57452.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS57452.1,
RC   ECO:0000313|Proteomes:UP000051182};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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|ARBA:ARBA00004496,
CC       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:KQS57452.1}.
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DR   EMBL; LMPZ01000001; KQS57452.1; -; Genomic_DNA.
DR   RefSeq; WP_056098342.1; NZ_LMPZ01000001.1.
DR   AlphaFoldDB; A0A0Q5VAD1; -.
DR   STRING; 1736353.ASG17_01645; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000051182; 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:UP000051182};
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   862 AA;  93690 MW;  F63CF9FC57AF0F9B CRC64;
     MNLDLYSDRA KQAVQSAQSL ALARRHQQFA PEHLLKVLLE ERDGLARNLI TAAGGDAKRA
     ETDVETALSK RAQVSGGSGQ LYLDGDTARV FAAAEAASKK AGDQFVTTER LLSALAREGG
     VAATVLKAAG VDAAKLDAAI ADVRKGKTAD SAGAEDGYDA LKRYARDLTL AARDGKIDPV
     IGRDEEIRRT IQVLARRTKN NPVLIGEPGV GKTAIVEGLA LRIVNGDVPE SLRDKTVMAL
     DMGSLIAGAK YRGEFEERLK AVLNEVSAAE GGIILFIDEM HTLVGAGKSD GAMDASNLLK
     PALARGELHC VGATTLDEYR KHVEKDAALA RRFQPVFVAE PSVEDTVSIL RGLKEKYEVH
     HGVRISDSAI VAAATLSNRY ITDRFLPDKA IDLVDEAASR VRMAVDSKPE ALDEIDRRLV
     QLKIEREALK KETDSASQNR LERLEDEISD LEVESHDLTT RWKAEKDKVG QGAQLRETLD
     RLRIELANAQ RAGDLGRASE IAYGQIPQIE RQLAEAEAAE TKGSGPLTPE VVDAEQIAQV
     VSRWTGVPVD KMLEGEREKL LHMEDALANR VVGQGPALAA VSDAVRRARA GLNDPNRPLG
     SFLFLGPTGV GKTELTKALA AFLFDDDAAI TRIDMSEYME KHSVSRLIGA PPGYVGYDEG
     GALTEAVRRR PYQVILFDEV EKAHPDVFNV LLQVLDDGRL TDGQGRVIDF KNTLIILTSN
     LGSEALAGQG EGDDVEAVRP YVMDQVRAHF RPEFLNRIDE IILFRRLGRD QMAGIVRIQL
     ARLEKLMADR RLTLSLDDTA AAWLADKGYD PVYGARPLKR VIQKELVDPM AKKLLAGELE
     DGSVIAVSAG SEGLEIGKAR VH
//
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