ID A0A1G7AVI3_9PROT Unreviewed; 864 AA.
AC A0A1G7AVI3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05421720_104109 {ECO:0000313|EMBL:SDE18849.1};
OS Rhodospira trueperi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospira.
OX NCBI_TaxID=69960 {ECO:0000313|EMBL:SDE18849.1, ECO:0000313|Proteomes:UP000199412};
RN [1] {ECO:0000313|EMBL:SDE18849.1, ECO:0000313|Proteomes:UP000199412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700224 {ECO:0000313|EMBL:SDE18849.1,
RC ECO:0000313|Proteomes:UP000199412};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|ARBA:ARBA00004496,
CC 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; FNAP01000004; SDE18849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7AVI3; -.
DR STRING; 69960.SAMN05421720_104109; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199412; 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:SDE18849.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDE18849.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199412};
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 864 AA; 93931 MW; 70633580F38CD886 CRC64;
MDFEKLTDRA KGFLQAAQTI AVREHHQQVT PEHLLKALLD DPEGMAASLI AAAGGDVEKA
KSGIDMAVGK QPRVEGASSM YWAQQTTRLL DQAQQIAEKA GDSFVTVERI LLALALAKGS
PAAKVLADAG VTPQGLNTAV ERLRKGRTAD SAGAENQYDA LKKYARDLTA AAREGKLDPV
IGRDDEIRRT VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA LRIINGDVPE SLRDKALMVL
DLGAMVAGAK YRGEFEERLK ALLSEIASSD GEYVLFIDEM HTLVGAGRAE GSMDASNLLK
PALARGELHC IGATTLDEYR KHVEKDAALA RRFQPVFVSQ PTVEDTVSIL RGIKEKYELH
HGVRIADAAL VAAATLSNRY ITDRFLPDKA IDLVDEAAAR LRMQVDSKPE PLEDLDRRVI
QLKIEREALK KESDPASRER LGKLEDELGD LEAKAAAMAA DWERQKGALA GTTALKEQLD
RARGELDIAR REANWARAGE LEYGVIPGLQ KQLEDAETSQ GDALLNEVVT EETVAAVVSR
WTGIPVDKML TGERDKLLAM ETALANRVVG QAEAVSAVSN AVRRARAGLG DPNRPIGSFL
FLGPTGVGKT ELTKALAAFL FDDETALIRV DMSEYMEKHA VARLIGAPPG YVGYDEGGAL
TEAVRRRPYQ VVLFDEVEKA HPDVFNVLLQ VLDEGRLTDG QGRVVDFKNT LIVMTSNLGA
DVLASQAEGE DSSAVRGLVM EQVQAAFRPE FLNRLDEILL FHRLFREHMA GIVDIQIARL
AKRLEDRGII LEMDTSARAW LAERGYDPVY GARPLKRVIQ RHLENPLAMM VLEGKIGDGD
TARVSAGEGG LIVNGKALEQ PAAA
//