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Database: UniProt
Entry: A0A2R8B9Q9_9RHOB
LinkDB: A0A2R8B9Q9_9RHOB
Original site: A0A2R8B9Q9_9RHOB 
ID   A0A2R8B9Q9_9RHOB        Unreviewed;       871 AA.
AC   A0A2R8B9Q9;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB_1 {ECO:0000313|EMBL:SPH19768.1};
GN   Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=ASD8599_00504 {ECO:0000313|EMBL:SPH19768.1};
OS   Ascidiaceihabitans donghaensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Ascidiaceihabitans.
OX   NCBI_TaxID=1510460 {ECO:0000313|EMBL:SPH19768.1, ECO:0000313|Proteomes:UP000244880};
RN   [1] {ECO:0000313|EMBL:SPH19768.1, ECO:0000313|Proteomes:UP000244880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8599 {ECO:0000313|EMBL:SPH19768.1,
RC   ECO:0000313|Proteomes:UP000244880};
RA   Keele B.F.;
RL   Submitted (MAR-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}.
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DR   EMBL; OMOR01000001; SPH19768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8B9Q9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000244880; 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:UP000244880};
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   871 AA;  95139 MW;  57AB163F32C1A175 CRC64;
     MDLSKFTERS RGFIQAAQTI ATRDSHQRLV PDHILKALMD DDQGLASNLI ASAGGDPKAV
     LTAVDVGLNK LPKVSGDAAQ VYLDQATNKV LAEAEAIAKK AGDSFVPVER ILMALCMVKS
     GAKTALEAGK VNAQALNAAI NDIRKGRTAD SASAEDGYDA LKKYAQDLTS RAEEGKIDPI
     IGRDEEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGMA LRIVNGDVPE SLRNKRLLSL
     DMGALIAGAK YRGEFEERLK AVLTEVTEAA GEIVLFIDEM HTLVGAGKAD GAMDAANLIK
     PALARGELHC IGATTLDEYR KYVEKDAALA RRFQPVVIAE PTVEDTVSIL RGIKEKYELH
     HGVRISDSAL VTAATLSHRY ITDRFLPDKA IDLVDEAASR LRMEVDSKPE ELDALDREIL
     QKQIEAEALR LEDDAASVDR LETLEKDLAD LQDRSAEMTA KWQSERDKMA GARDLKEQID
     RARAELDIAK REGNLGKAGE LSYGVIPELE RKLGEAEGAE TEAMVAEAVR PEQIASVVER
     WTGIPTAKML EGDREKLLRM EDQLHSRVIG QHKAVQALSN AVRRSRAGLN DEDRPLGSFL
     FLGPTGVGKT ELTKAVAEFL FDDDSAMVRI DMSEFMEKHA VSRLIGAPPG YVGYDEGGVL
     TEAVRRRPYQ VVLFDEVEKA HPDVFNVLLQ VLDDGVLTDG QGRTVDFKQT LIILTSNLGA
     QALSQLPDGA DASDAKRDVM DAVRAHFRPE FLNRLDETII FDRLNRKDMD GIVDIQMARL
     LRRLAARKIT LDLDDGARTW LADEGYDPVF GARPLKRVIQ NALQNPLAEM LLAGDLKDGD
     TLAVSAGVEG LVIGDRIGSS NRAKPDEATV H
//
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