ID A0A1G4QJS4_9CAUL Unreviewed; 860 AA.
AC A0A1G4QJS4;
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=SAMN02927928_1307 {ECO:0000313|EMBL:SCW44873.1};
OS Asticcacaulis taihuensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=260084 {ECO:0000313|EMBL:SCW44873.1, ECO:0000313|Proteomes:UP000199150};
RN [1] {ECO:0000313|EMBL:SCW44873.1, ECO:0000313|Proteomes:UP000199150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3431 {ECO:0000313|EMBL:SCW44873.1,
RC ECO:0000313|Proteomes:UP000199150};
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; FMTS01000001; SCW44873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4QJS4; -.
DR STRING; 260084.SAMN02927928_1307; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199150; 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:SCW44873.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SCW44873.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..490
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 860 AA; 94503 MW; 4BF4570A3022EDAC CRC64;
MNIEKYSEKT QKLIQSAQGI AQARNHQYFT PVHVLKALTE DKDSLSSQLI QLAGGRADAF
AASIDLALGK LPAVTGAGQL YMANETAKLF NDAEAEANKA GDSFVTADRL LIAAADNKEG
AEALKAAGIS LGKLKDAQAA FRKGKPADSA SAEAGFDALK KYARDLTQAA LDGKIDPVIG
RDEEIRRTIQ VLARRTKNNP VLIGEPGVGK TAIVEGLAQR IVNGDVPESL KDKKLLSLDM
GALIAGAKYR GEFEERLKAV LNEVTQAEGQ IVLFIDEMHT LVGAGKSDGA MDASNLLKPA
LARGELHCVG ATTLDEYRKH VEKDPALARR FQPVFVTEPT VEDTISILRG LKEKYEVHHG
VRISDSAIVS AATLSNRYIA DRFLPDKAID LIDEAASRVR MAVDSKPEEL DELDRRIVQL
KIEREALQKE TDAGSKTRLE KLSEELEELE EKSLALTTRW KAEKDKVGSA ARSREALDRA
RIDLANAQRA GDLQKASEIM YGIIPALEKA LEREENAPQG EESPLTPEVV DSTQIAQVVS
RWTGIPVDKM LEGERDKLLR MEDVLRGRVV GQDEALTAVA DAVRRARAGL KDPNRPIGSF
LFLGPTGVGK TELNKALAEF LFDDETAITR LDMSEYMEKH SVSRMIGAPP GYVGYDEGGA
LTEAVRRRPY QVVLFDEVEK AHPDVFNILL QVLDDGRLTD GQGRVVDFRN TLIVMTSNLG
SDVLVNMEPD GDIEVVRPLV LNAVRKHFRP EFLNRIDEMI LFHRLDRAHM HDIVRIQLKG
LEKLLADREM TLSIDDAALN YLADKGYDPA YGARPLKRVI QKLLVDEIAR KILSGEVTDG
EVIHVGFDGE HLTIGKPTVN
//