ID A0A0D6PKY4_9PROT Unreviewed; 859 AA.
AC A0A0D6PKY4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=Aam_126_002 {ECO:0000313|EMBL:GAN81873.1};
OS Acidocella aminolytica 101 = DSM 11237.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidocella.
OX NCBI_TaxID=1120923 {ECO:0000313|EMBL:GAN81873.1, ECO:0000313|Proteomes:UP000032668};
RN [1] {ECO:0000313|EMBL:GAN81873.1, ECO:0000313|Proteomes:UP000032668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=101 / DSM 11237 {ECO:0000313|Proteomes:UP000032668};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidocella aminolytica 101 = DSM 11237.";
RL Submitted (NOV-2012) 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:GAN81873.1}.
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DR EMBL; BANC01000124; GAN81873.1; -; Genomic_DNA.
DR RefSeq; WP_048880257.1; NZ_FQVJ01000022.1.
DR AlphaFoldDB; A0A0D6PKY4; -.
DR STRING; 1120923.SAMN02746095_02429; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000032668; 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:GAN81873.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:GAN81873.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032668};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 859 AA; 94430 MW; 5FA99FA59593B6C8 CRC64;
MDFEKFTERA RGFIQAAQTI AMREYNQQIT PEHLLKAFLD DEEGAASGLI RMAGGDPAGV
KQIVDAAVAK LPKVSGSGAG QPGVTPDLVR VLDAAQQAAT KAGDSFVAQD RILVALAVTD
NAAGRALKAA GVSAQALEKA VNDVRKGRKV DSATAEQQFD ALKKYARDVT QLARDQKLDP
VIGRDEEIRR TIQVLARRTK NNPVLIGEPG VGKTAIVEGL ALRIVNGDVP ESLRNKRVLA
LDMGALVAGA KFRGEFEERL KAVLKEIESA EGEIILFIDE MHTLVGAGKA DGAMDASNLL
KPELARGALH CVGATTLDEY RKYVEKDAAL ARRFQPVFVD EPSVEDTISI LRGIKEKYEL
HHGVRITDNA LVAAATLSNR YITDRFLPDK AIDLVDEASS RLRMQVDSKP EALDELDRRL
IQLKIEREAL KKETDAASRD RLEKLEFELG ELEERSSEMT AKWKAEKAEH AEVQKVQEQL
DQARNEVEMA QRKGDLGKAS ELLYGRIPEL EKLLAAKQDG TMVTEAVTEE AIAAVVSRWT
GVPVEKMLEG ERAKLLHMED NLRNRVVGQE AALVAVSNAV RRARAGLQDP NRPIGSFLFL
GPTGVGKTEL TKALAEFLFD DERAMVRIDM SEFMEKHSVS RLIGAPPGYV GYDEGGVLTE
AVRRRPYQVV LFDEVEKAHE DVFNVLLQVL DDGRLTDGQG RTVDFKNTII VLTSNLGSDI
LAAQKEGEDV RMAEAGVMAR VREHFRPEFL NRLDEIVLFR RLQRVDMGSI VTIQLKRLEG
LLAERNIRLD LDQSARDWLA EAGYDPVYGA RPLKRVIQRN LQNPLAGLIL EGAVKDGDTV
KVSGSDQGLV IGGHLAEAA
//