ID A0A0C4YFY9_9BURK Unreviewed; 896 AA.
AC A0A0C4YFY9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=ClpB protein {ECO:0000313|EMBL:AJG21848.1};
GN ORFNames=RR42_s0252 {ECO:0000313|EMBL:AJG21848.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG21848.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG21848.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG21848.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
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 -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675}.
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DR EMBL; CP010537; AJG21848.1; -; Genomic_DNA.
DR RefSeq; WP_043353022.1; NZ_CP010537.1.
DR AlphaFoldDB; A0A0C4YFY9; -.
DR STRING; 68895.RR42_s0252; -.
DR KEGG; cbw:RR42_s0252; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000031843; Chromosome secondary.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR017729; ATPase_T6SS_ClpV1.
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; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03345; VI_ClpV1; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF181; ATPASE SUBUNIT OF ATP-DEPENDENT PROTEASE-RELATED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031843};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 10..161
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 166..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 896 AA; 96488 MW; 8F2B82AC5585871C CRC64;
MTARDLSAFL RRLNDHCARA LADAASLCET RAHRDIEVEH WLIKLLELGD GDLLAILRRY
ELDVDGIWNG LLAAIDRLPH DLRGKPGLSQ RLGQWLEAAW MRASLEAATP GESTSIRSAH
LLAALTETPH LLRAPGAWPL LSVSAVQIER LMHELDKIST EAAARGAGEP ARPDCAPLSS
VPVTPAAPAP TRSMPGQADA SALARFTTDV TQKARDGKID PVFGRDVEIR QMVDILARRR
KNNPILVGEP GVGKTALVEG LALNIAQGNV PAVIQNVSVL TLDLGLLQAG AGVKGEFEQR
LKNVIEAVQQ SPTPVLLFID EAHTLIGAGN TAGGADAANL LKPALARGEL RTIAATTWSE
YKQYFERDAA LERRFQMVKV DEPDDDGACL MLRGLKERYA QHHGVHITDA AVAAAVRLSR
RYLSGRQLPD KAVDLLDTAA ARVRMSLEAT PVAISSREAQ RAALEVERTA LLHDQGAIDA
RLAALAIELE QFERAFAEQK GAAETLIALR ARWQSAADES ARQDLTPSIQ AAHEMLTRHG
QAALIHAEVD ETAIAQVIAD WTGVPVDSLL SSELATLLAL EARLGHIVVG QDEALAALSK
SLRAAKAGLK SEEAPLGVFL LVGPSGVGKT ETARALADLM FGGERSLVTI NLSEYQEAHT
VSQLKGSPPG YVGYGEGGVL TEAVRQRPYS VILLDEVEKA HRDVLNLFYQ VFDRGFMRDG
EGRVIDFRNT VILMTSNLGS EQILAATDAA VTAGAELATG TLMEAIRPML IDHFQPALLA
RFQTIVYRPL SAHAMAMIVR MKLGKVAERI ARRFGVPLRC GDTLVDELVR ACLLPDSGAR
NIDTLLDQQI LPVLSRELLV RMSGQQVPAS IHLSFSEGDG IGLEFEEPAT TAGAGA
//