ID A0A2G8SYR3_9BURK Unreviewed; 872 AA.
AC A0A2G8SYR3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:PIL38930.1};
GN ORFNames=CR103_15380 {ECO:0000313|EMBL:PIL38930.1};
OS Massilia psychrophila.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1603353 {ECO:0000313|EMBL:PIL38930.1, ECO:0000313|Proteomes:UP000228593};
RN [1] {ECO:0000313|EMBL:PIL38930.1, ECO:0000313|Proteomes:UP000228593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 30813 {ECO:0000313|EMBL:PIL38930.1,
RC ECO:0000313|Proteomes:UP000228593};
RA Wang H.;
RT "Massilia psychrophilum sp. nov., a novel purple-pigmented bacterium
RT isolated from Tianshan glacier, Xinjiang Municipality, China.";
RL Submitted (OCT-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:PIL38930.1}.
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DR EMBL; PDOB01000026; PIL38930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8SYR3; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000228593; 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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000228593};
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 872 AA; 96816 MW; B3488AC4DC233679 CRC64;
MRQDKITTKL QEALSDAQSL AVGNDNQYIE PVHLLTALLN QDDGGARSLF LRAGVNVGAM
TNALKSALER LPKVSGTGGE TQIGRELMAV LNLADKEAQK RGDQFIASEM VLLALTEDKS
DCGRLAREAG LTRKALELAI DAVRGGEAVN SQDAEGQRES LKKYTLDLTE RARQGKLDPV
IGRDDEIRRT IQILQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPD SLKGKRVLSL
DMAALLAGAK YRGEFEERLK SVLKELAQDE GQTIVFIDEM HTMVGAGKAE GAMDAGNMLK
PALARGELHC VGATTLDEYR KYIEKDAALE RRFQKVLVEE PTVEATIAIL RGLQDKYELH
HKVQITDPAI IAAAELSHRY ITDRFLPDKA IDLIDEAAAK IKIEIDSKPE VMDRLERRII
QLKIEKEAVK KEKDEASQRR LGLIDDEIAR LEREYNDYEE ILKAEKAMVQ GTTHIKEEIE
RIRHQMEEAK RQSDYALMSE LQYGKLPELE AQLKHAEDAT ALNAVGAKPK LLRTQVGAEE
IAEVVSRATG IPVSRMMQGE REKLLHIEDR LHQRVVGQDE AIEAVSDAIR RSRAGLADPS
RPYGSFMFLG PTGVGKTELC KALASFLFDT EESMIRIDMS EFMEKHSVAR LIGAPPGYVG
YDEGGYLTEA VRRRPYSVIL FDEIEKAHQD VFNVLLQVLD DGRMTDGQGR TVDFKNTVIV
MTSNLGSHKI QSMESDDPGV VKLAVMAEVR NHFRPEFINR IDEIVVFHAL DEKNIGAIAK
IQLRQLEGRL EKMDMALVVS KEALQKIAEA GYDPVYGARP LKRAIQQQIE NPLSKLILSG
KFGPKDTITV GVERGSLVFG EPQTVALEKI PG
//
