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Database: UniProt
Entry: A0A1G4QJS4_9CAUL
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Original site: A0A1G4QJS4_9CAUL 
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
//
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