GenomeNet

Database: UniProt
Entry: A0A562B3D2_9BURK
LinkDB: A0A562B3D2_9BURK
Original site: A0A562B3D2_9BURK 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system