ID A0A518RGF3_9SPHN Unreviewed; 859 AA.
AC A0A518RGF3;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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:QDX26537.1};
GN ORFNames=FPZ54_11215 {ECO:0000313|EMBL:QDX26537.1};
OS Sphingomonas suaedae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2599297 {ECO:0000313|EMBL:QDX26537.1, ECO:0000313|Proteomes:UP000318055};
RN [1] {ECO:0000313|EMBL:QDX26537.1, ECO:0000313|Proteomes:UP000318055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XS-10 {ECO:0000313|EMBL:QDX26537.1,
RC ECO:0000313|Proteomes:UP000318055};
RA Zhang H., Xu L., Zhang J.-X., Sun J.-Q.;
RT "Sphingomonas alkalisoli sp. nov., isolated from rhizosphere soil of
RT Suaedae salsa.";
RL Submitted (JUL-2019) 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; CP042239; QDX26537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A518RGF3; -.
DR KEGG; ssua:FPZ54_11215; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000318055; Chromosome.
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:UP000318055};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 415..495
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 859 AA; 93872 MW; F46F9F9578F13AD5 CRC64;
MNLEKFTDRA KGFLQSAQTV AIRMNHQRIS PEHLLKALLE DEQGMAAGLI QAAGGDAKRA
VAETDAALSR VPAVTGSGAQ QAPGLDNDAV RVLDQAEQIA GKAGDSYVTV ERMLLALTLA
MTTNAGRALA AAGVKPEALN AAINQLRGGR TADTAGAEDR YDALKKFARD LTQAAKDGKL
DPVIGRDEEI RRTIQILARR TKNNPVLIGD PGVGKTAIAE GLALRIANGD VPDTLKDRRL
MALDMGSLIA GAKYRGEFEE RLKGVLDEVK GAEGDIILFI DEMHTLIGAG KSEGAMDAGN
LLKPALARGE LHCIGATTLD EYRKYVEKDP ALQRRFQPVF IGEPTVEDTI SILRGLKEKY
ELHHGVRITD GAIVSAATLS NRYISDRFLP DKAIDLMDEA ASRIRMEVES KPEEIETLDR
RIVQLKIEEM ALAKETDAAS QDRLVNLRHE LANLEQQSAE LTQRWQAEKD KIAGEAKIKE
QLDAARLELE QAQRAGDLAK MAELNYGTIP SLTKQLEEAQ ATTGSAMLRE EVTADDIAGV
VSRWTGIPVD RMLEGEREKL LAMEEQLGKR VIGQAAAVKA VSTAVRRSRA GLQDPNRPLG
SFLFLGPTGV GKTELTKALA EFLFDDSSAM VRIDMSEFME KHSVARLIGA PPGYVGYEEG
GVLTEAVRRR PYQVVLFDEV EKAHGDVFNI LLQVLDDGRL TDGQGRTVDF TNTIVVLTSN
LGSQFLTQLE DGQDVSSVEP QVMEIVRAHF RPEFLNRLDE IVLFHRLGRD EMAPIVDIQV
ARLGHLLKDR KIVLELTPEA RDWLGRVGYD PVYGARPLKR AVQRYLQDPL ADAILRGEVK
DGATVKVSEG DGGLVLTPV
//