ID A0A1U7DI43_9RHOB Unreviewed; 872 AA.
AC A0A1U7DI43; A0A2M9DD03;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BV394_07975 {ECO:0000313|EMBL:APX89660.1}, CLV77_0181
GN {ECO:0000313|EMBL:PJJ85661.1};
OS Brevirhabdus pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Brevirhabdus.
OX NCBI_TaxID=1267768 {ECO:0000313|EMBL:APX89660.1, ECO:0000313|Proteomes:UP000187266};
RN [1] {ECO:0000313|EMBL:APX89660.1, ECO:0000313|Proteomes:UP000187266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6-4 {ECO:0000313|EMBL:APX89660.1,
RC ECO:0000313|Proteomes:UP000187266};
RA Wang X.;
RT "Genomic analysis of Xuhuaishuia manganoxidans DY6-4.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PJJ85661.1, ECO:0000313|Proteomes:UP000229573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27767 {ECO:0000313|EMBL:PJJ85661.1,
RC ECO:0000313|Proteomes:UP000229573};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-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}.
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DR EMBL; CP019124; APX89660.1; -; Genomic_DNA.
DR EMBL; PGFI01000011; PJJ85661.1; -; Genomic_DNA.
DR RefSeq; WP_076979683.1; NZ_PGFI01000011.1.
DR AlphaFoldDB; A0A1U7DI43; -.
DR STRING; 1267768.BV394_07975; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000187266; Chromosome.
DR Proteomes; UP000229573; 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:PJJ85661.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PJJ85661.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187266};
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..496
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 96189 MW; A23489AC6CF995F3 CRC64;
MNLEKFTERS RGFLQAAQTI AMRESHQKLA PEHLLKALLD DEEGLATNLI RRAGGEPERV
VESVELALGK LPKVTGDAGQ TYMDQQTGKV LDEAEKIAKK AGDSYVAVER ILTALAVVKS
KAREALEAGA ITAQKLNTAI NDVRKGRTAD SANAEEGYDA LKKYARDLTE AAEQGRIDPI
IGRDEEIRRT MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLRNKRLMAL
DMGSLIAGAK YRGEFEERLK AILKEIEAAA GEIILFIDEM HTLVGAGKTD GAMDASNLLK
PALARGELHC VGATTLDEYR KHVEKDAALA RRFQPVMVEE PTVEDTISIL RGIKEKYELH
HGVRISDAAL VAASTLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ALDALDRDIL
QKQIEAEALK KEDDDASKGR LEKLEKELSD LMERSSEMTA KWQAERDKLE SARTVKERLD
RARAELEQAK REGNLQKAGE LSYGVIPDLE RQVKGSDGGE AEDMMVEEAV RPEQIAQVVE
RWTGIPTSKM LEGEREKLLK MEEQLGRRVV GQDRAVKAVA NAVRRARAGL NDENRPLGSF
LFLGPTGVGK TELTKAVAEY LFDDDSAMVR IDMSEFMEKH AVSRLIGAPP GYVGYDEGGV
LTEAVRRRPY QVVLFDEVEK AHPDVFNVLL QVLDDGVLTD GQGRTVDFKQ TLIVLTSNLG
SHALGQQAEG EDSAAAHAAV MEAVRGHFRP EFLNRLDETI IFDRLSREDM TGIVDIQLER
LTKRLAARNI TLEMDEAARK WLADEGYDPV FGARPLKRVI QRALQDQLAE MILSGDVHDG
DTIPVSAGTD GLVVGDRVAT SNRRPPSEAV VH
//
