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Database: UniProt
Entry: A0A6I4YU04_9PROT
LinkDB: A0A6I4YU04_9PROT
Original site: A0A6I4YU04_9PROT 
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}.
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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
//
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