ID A0A317EAR8_9PROT Unreviewed; 882 AA.
AC A0A317EAR8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PWR22393.1};
GN ORFNames=DKG75_10630 {ECO:0000313|EMBL:PWR22393.1};
OS Zavarzinia compransoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Zavarziniaceae; Zavarzinia.
OX NCBI_TaxID=1264899 {ECO:0000313|EMBL:PWR22393.1, ECO:0000313|Proteomes:UP000246077};
RN [1] {ECO:0000313|Proteomes:UP000246077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1231 {ECO:0000313|Proteomes:UP000246077};
RA Lee Y., Jeon C.O.;
RT "Zavarzinia sp. HR-AS.";
RL Submitted (MAY-2018) 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}.
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:PWR22393.1}.
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DR EMBL; QGLF01000002; PWR22393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317EAR8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000246077; 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:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000246077};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 882 AA; 96285 MW; A74AD4CAA24CA445 CRC64;
MDFEKYTERA RGFVQSAQGL ALRSNHQRFT PEHLAKVLLD DEQGLAASLI KAAGGRPEAA
LAGIEAELAR LPKVEGQGAG QLYLAPETAR LFEQAEQVAK KAGDTFVTAE RLLLALVLAA
GTPSAEILKK AGVTAQGLSK AIDDLRKGRT ADSASAEDSY DALKKYARDL TAAARDGKLD
PVIGRDEEIR RTIQVLSRRT KNNPVLIGEP GVGKTAIAEG LALRIVNGDV PESLKHKQLM
ALDLGALVAG AKYRGEFEER LKAILGEVTS SGDVILFIDE MHQLVGAGKT DGAMDASNLL
KPALARGELH CVGATTLDEY RKHVEKDAAL ARRFQPVFVS EPTVEDTISI LRGLKEKYEL
HHGVRISDVA LVAAATLSNR YITDRFLPDK AIDLVDESAS RLRMEVDSKP EALDELDRKI
MQMQIEREAL KKEEDRASKE RLAKLEKDLA DLEQQSAEMT AKWRAEKDKL SVQQKLTEQL
DAARSELEQA QRKGNLARAG EIAYGLIPDL TRKLEAAQAA TEAASMREAV TDEDIAAVVS
RWTGIPVDKM LSGEREKLLK MEPLLASRVV GQPEAVAAVA NAVRRARAGL QDAARPIGSF
LFLGPTGVGK TELTKALAEF LFDDDTAMVR VDMSEFMEKH AVSRLIGAPP GYVGYEEGGV
LTEAVRRRPY QVILFDEVEK AHPDVFNVLL QVLDDGRLTD GQGRTVDFRN TVIILTSNLG
GEFLAAEDAE VNPGRTRDQV MAVVRASFRP EFLNRLDEIV LFNRLGRGEM TGIVDIQLGR
LRKLLADRKI VLDLDQAAKE WLAEAGYDPV YGARPLKRVI QRNLQNPLAE LILEGEVNDG
DTVKVSAEAG QLVLNGKAVE ADNALVRKPS NPAFVSRVEG NA
//