ID A0A1M5L4W6_9BURK Unreviewed; 871 AA.
AC A0A1M5L4W6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05428948_1224 {ECO:0000313|EMBL:SHG60031.1};
OS Massilia sp. CF038.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1881045 {ECO:0000313|EMBL:SHG60031.1, ECO:0000313|Proteomes:UP000184361};
RN [1] {ECO:0000313|EMBL:SHG60031.1, ECO:0000313|Proteomes:UP000184361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF038 {ECO:0000313|EMBL:SHG60031.1,
RC ECO:0000313|Proteomes:UP000184361};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQWU01000001; SHG60031.1; -; Genomic_DNA.
DR RefSeq; WP_073213197.1; NZ_FQWU01000001.1.
DR AlphaFoldDB; A0A1M5L4W6; -.
DR STRING; 1881045.SAMN05428948_1224; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000184361; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 78, MITOCHONDRIAL; 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 Hydrolase {ECO:0000313|EMBL:SHG60031.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SHG60031.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184361};
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..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 96811 MW; 36B409A4076D16BF CRC64;
MRQDKITTKL QEALSDAQSL AVGGDNQYIE PVHLLLALLN QDDAGARSLL QRAGVNVGGL
TTNLKNALER LPKVSGTGGE TQVSRELMNV LNLADREAQK RSDQFISSEM VLLALTDDKS
EAGKLAREHG LSRKALEAAI QAVRGGESVN SAESEGQREA LKKYTLDLTE RARMGKLDPV
IGRDDEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNNEVPD SLKGKRVLSL
DMAALVAGAK FRGEFEERLK SVLKELAQDE GQTIVFIDEM HTMVGAGKAD GAMDAGNMLK
PALARGELHC VGATTLDEYR KYIEKDAALE RRFQKILVDE PSVEATIAIL RGLQDKYELH
HKVEITDAAI IAAAELSHRY ITDRFLPDKA IDLIDEAASK IKIEIDSKPE VMDKLERRII
QLKIEKEAVK KEKDEASRRR LDLIDEEIAR LEREYNDFEE VLKSEKAMVQ GTTHIKEEIE
RIRHEMEEAT RASNWQKVSE LQYGRLPELE AQLKSAESDA ARQENAAQPK LLRTQVGAEE
IAEVVSRATG IPVSRMMQGE RDKLLHIEEK LHERVVGQDE AIVAVADAIR RSRAGLSDPN
RPYGSFMFLG PTGVGKTELC KALANFLFDT EESMIRIDMS EFMEKHSVAR LIGAPPGYVG
YDEGGYLTEA VRRKPYSVIL LDEVEKAHSD VFNVLLQVLD DGRMTDGQGR TVDFKNTVIV
MTSNLGSHKI QSMDSDDPGV VKLAVMAEVR SHFRPEFINR IDEIVVFHAL DEKNIGAIAK
IQLQHLEQRL AKMEMTLDIN DAALQKIAEA GYDPVYGARP LKRAIQQQIE NPLSKLILAG
KFGPKDTIPV RVEHGNLVFE TKAGAVELDK V
//
