ID A0A0Q5Z9U9_9BURK Unreviewed; 874 AA.
AC A0A0Q5Z9U9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ASG30_10180 {ECO:0000313|EMBL:KQT10216.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT10216.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT10216.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10216.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT10216.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10216.1,
RC ECO:0000313|Proteomes:UP000051173};
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|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:KQT10216.1}.
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DR EMBL; LMQL01000011; KQT10216.1; -; Genomic_DNA.
DR RefSeq; WP_055897820.1; NZ_LMQL01000011.1.
DR AlphaFoldDB; A0A0Q5Z9U9; -.
DR STRING; 1736365.ASG30_10180; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051173; 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:UP000051173};
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; 97018 MW; 7252C80A7B5B7A78 CRC64;
MRLDKLTTKF QEALGEAQSL ALANDHAYIE AEHLMVAMLR QEDGPRSLLQ RAGVNVPGLQ
ATAEAAMHKR PQVQGQEQVQ VGRELVTLLQ AAEKEGLKRG DQFIASELFL LAVADSKADI
GRIARENGLT RKSLESAVDA VRGGQSVDSA GSEGQREALK KYTVDLTERA QRGKLDPVIG
RDEEIRRAIQ VLQRRTKNNP VLIGEPGVGK TAIVEGLAQR IVAGEVPESL KNKRVLSLDM
AALLAGAKYR GEFEERLKNV LTELAKDEGR TIVFIDELHT MVGAGKAEGA MDAGNMLKPA
LARGELHCVG ATTLDEYRKY IEKDAALERR FQKILVGEPT VEATIAILRG LQEKYEVHHG
VEITDPAIVA AAELSHRYIT DRFLPDKAID LIDEAASKIK IEIDSKPEAI DRLDRRLIQL
QIEREAVRKE KDEASQKRLG LIEDEITRLQ KEIADLEEIW KAEKASAQGS AQVKEEIDRA
RFQIEEFKRK ADFNKVAELQ YGRLPELERK LKAAQDAETG KAKAGRPQLL RTQVGAEEIA
EVVARSTGIP VSKLMQGERE KLLQMEERLH QRVVGQDEAI SAVANAIRRS RSGLSDPNRP
TGSFLFLGPT GVGKTELCKA LANFLFDSEE HLIRVDMSEF MEKHSVARLI GAPPGYVGYE
EGGYLTEAVR RKPYSVILLD EVEKAHHDVF NVLLQVLDDG RLTDGQGRTV DFKNTVIAMT
SNIGSHMIQA MAGRPYEDVK DAVWDELKNH FRPELLNRID ETVVFHGLGA DHIARIAQIQ
LKVLEQRLAK MDLTLQVSPA ALEELAKVGF DPVYGARPLK RAIQQRIENP LSRLILEGRF
PPKSAIPVEV DPVREPGVFH FGPVKAEPRE QAPA
//