ID A0A562B3D2_9BURK Unreviewed; 862 AA.
AC A0A562B3D2;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=L602_000600000560 {ECO:0000313|EMBL:TWG79656.1};
OS Cupriavidus gilardii J11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=936133 {ECO:0000313|EMBL:TWG79656.1, ECO:0000313|Proteomes:UP000318141};
RN [1] {ECO:0000313|EMBL:TWG79656.1, ECO:0000313|Proteomes:UP000318141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J11 {ECO:0000313|EMBL:TWG79656.1,
RC ECO:0000313|Proteomes:UP000318141};
RA Gladden J.;
RT "Genome sequencing of lignin-degrading bacterial isolates.";
RL Submitted (JUL-2019) 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:TWG79656.1}.
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DR EMBL; VLJN01000056; TWG79656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A562B3D2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000318141; 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 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 Hydrolase {ECO:0000313|EMBL:TWG79656.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TWG79656.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000318141};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 411..491
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 95604 MW; 7340BB93985F9FB8 CRC64;
MRLDKLTTRF QEALADAQSL AIANDNQYID PLHVLRALLS QNDGAARSLL SRAGVNVNGL
GNALDAAIKR LPQVQGTSEV QVGRELAALL NATEKEAMKR GDQFIASELF LLAVADDKGE
AGRVAREHGL ARKSLEAAID AVRGGDAVNS ADAESQREAL KKYTIDLTER ARMGKLDPVI
GRDDEIRRSI QILQRRTKNN PVLIGEPGVG KTAIVEGLAQ RIVNGEVPES LKNKRVLVLD
MAGLLAGAKY RGEFEERLKA VLSDIAKDEG QTIVFIDEIH TMVGAGKAEG AIDAGNMLKP
ALARGELHCI GATTLDEYRK YIEKDAALER RFQKVLVDEP SVEATIAILR GLQEKYELHH
GVEITDPAIV AAAELSHRYI TDRFLPDKAI DLIDEAAARI KMEIDSKPEA MDKLERRTIQ
LKIEREAVKK ETDEASRKRL ELIEQEIARL EKEYADLDEI WKAEKGAAQG AAALKEEIDK
IRLEISRLQR EGKLDKVAEL QYGKLPELEG KLRAATAAEA SEQKQPNRLL RTQVGAEEIA
EVVSRATGIP VSKMMQGERD KLIRMEDYLH RRVVGQDEAV RLVSDAIRRS RAGLADENKP
YGSFLFLGPT GVGKTELCKA LAEFLFDSEE HLIRIDMSEF MEKHSVARLI GAPPGYVGYE
EGGYLTEAVR RKPYSVVLLD EVEKAHPDVF NVLLQVLDDG RLTDGQGRTV DFKNTVIVMT
SNMGSQIIQS MAGEPHEAIK GAVWQEVKTQ FRPEFLNRID EVVVFHALDQ KHIESIARIQ
LQRLEARLAK LDMMLEVSDA ALEHIASAGY DPVFGARPLK RAIQQQIENP VARMILEGKF
AAKDVVPVDY QNGEFSFGRV VH
//