ID A0A6I4YU04_9PROT Unreviewed; 862 AA.
AC A0A6I4YU04;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:MXV36593.1};
GN ORFNames=GS535_08495 {ECO:0000313|EMBL:MXV36593.1};
OS Saccharibacter sp. EH611.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Saccharibacter.
OX NCBI_TaxID=2689391 {ECO:0000313|EMBL:MXV36593.1, ECO:0000313|Proteomes:UP000431119};
RN [1] {ECO:0000313|EMBL:MXV36593.1, ECO:0000313|Proteomes:UP000431119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EH611 {ECO:0000313|EMBL:MXV36593.1,
RC ECO:0000313|Proteomes:UP000431119};
RA Smith E.A., Vuong H.Q., Miller D.L., Parish A.J., Mcfrederick Q.S.,
RA Newton I.L.G.;
RT "Draft genomes of four Saccharibacter sp. strains.";
RL Submitted (DEC-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}.
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:MXV36593.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; WVHP01000022; MXV36593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6I4YU04; -.
DR Proteomes; UP000431119; 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:UP000431119};
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..527
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 94851 MW; 2A552960D259B97E CRC64;
MDIQKFTERS QGFIQAAQTI ALRDYHQQLT PEHLLKALLD DEQGAASALI RAAGGDPKQV
QTANDAALAK VPQVQGSGAS QPQATPDFVR VLDGAEADAQ AAGDSFVAQD RLLVAISRSK
TPAGDALRGG HATPEALAQA VEKIRKGRKV DSAGAESTFD ALKKYARDVT AVAREGKLDP
VIGRDEEIRR AVQVLARRSK NNPVLIGEPG VGKTAIVEGL ALRIINGDVP EALRNKSLLS
LDLGALVAGA KYRGEFEERL KAVLKEIESA EGEVILFIDE MHTIVGAGRS DGAMDASNLI
KPELARGVLH CIGATTLDEY RKYIEKDAAL ARRFQPVFVG EPSVTDTVSI LRGIKEKYEL
HHGVRITDNA LVAAATLSNR YITDRFLPDK AIDLVDEAAS RVRMQIDSKP EALDELDRRI
IQLKIEREAI RKEEDSASKE RLVALEAELA DLQEKSDELS AEWHAEKDRM GAVQKSKEKL
DQARSEVEIA QRQGNLQRAS ELMYSQIPQL EAEIAQAQEA AEASADKAGL FADTVTDQGI
AAVVSRWTGV PVDRMLEGER SKLLRMESVL RERVVGQETA LVAVSNAVRR ARAGLQDPNR
PIGSFLFLGP TGVGKTELTK TLAQFLFDDE NALLRIDMSE FMEKHSVSRL VGAPPGYVGY
DEGGVLTEAV RRRPYQVILF DEVEKAHPDV FNILLQVLDD GRLTDSQGRV VDFRNTIIVL
TSNLGSDVLS QQQDGEPTEQ VQDQVMSVVR EHFRPEFLNR LDEIILFSRL QRADMGKIVD
IQLGRLRKLL ADRKIELELD DKAREWLAAA GYDPVYGARP LKRVIQRELQ NELAELLLKG
TVHDGQTVLV SADDDHLVIS EK
//