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Database: UniProt
Entry: A0A0D6PKY4_9PROT
LinkDB: A0A0D6PKY4_9PROT
Original site: A0A0D6PKY4_9PROT 
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
//
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