ID A0A547P9F9_9SPHN Unreviewed; 858 AA.
AC A0A547P9F9;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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:TRD10769.1};
GN ORFNames=FGU71_02060 {ECO:0000313|EMBL:TRD10769.1};
OS Erythrobacter insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=2584124 {ECO:0000313|EMBL:TRD10769.1, ECO:0000313|Proteomes:UP000316343};
RN [1] {ECO:0000313|EMBL:TRD10769.1, ECO:0000313|Proteomes:UP000316343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBTF-M21 {ECO:0000313|EMBL:TRD10769.1,
RC ECO:0000313|Proteomes:UP000316343};
RA Yoon J.-H.;
RT "Erythrobacter insulae sp. nov., isolated from a tidal flat.";
RL Submitted (JUN-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:TRD10769.1}.
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DR EMBL; VHJK01000001; TRD10769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A547P9F9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000316343; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 858 AA; 94222 MW; 1AC0495F1D631C31 CRC64;
MNLEKFTDRA KGFLQSAQTV AIRMNHQRIT PLHLLKALLE DEEGMAAGLI QRAGGEATLA
VSAVDAGLSK IPAVTGGGAQ QTPGLDNDAV RALDSAEQLA DKAGDSYVTV ERVLTALALA
PGAAGEAMKA ASVTPQSLNA AIEDLRGGKK ADSANAESTY DAMEKFARDL TQAARDGKLD
PVIGRDEEIR RTIQILARRT KNNPALIGEP GTGKTAIAEG LALRIANGDV PDSLKGRTLM
SLDMGSLIAG AKYRGEFEER LKSVLDEVKN ADGQIILFID EMHTLIGAGA SEGSMDASNL
LKPALSRGEL HCIGATTLDE YQKYVEKDPA LQRRFQPVYI EEPSVEDTIS ILRGIKDKYE
LHHGVRITDG SIVAAARLSD RYIQNRFLPD KAIDLMDEAA SRIRMEVESK PEEIDELDRR
IIQLKIEESA LEKEDDAGSR DRLKALRDEL ANLEQDSSEL TTRWQNERDK IEAEGKIKEQ
LDAARLELEQ AQRTGDLAKA GELSYGTIPD LEKRLEAAED LTDDALLREE VTEEDIAGVV
ARWTGIPMER MMEGEREKLL DMENILGKRV IGQSDAIAAV SKAVRRARAG LQDPGRPLGS
FLFLGPTGVG KTELTKALAG FLFDDDSAMV RIDMSEFMEK HSVARLIGAP PGYVGYDEGG
VLTESVRRRP YQVVLFDEVE KAHSDVFNVL LQVLDDGRLT DGQGRVVDFS NTLIILTSNL
GSQFLSNLAD DQKVTEVEDQ VMDVVRGHFR PEFLNRLDEI ILFHRLAMEH MAPIVAIQVK
RVQKLLDDRK ITIDLTEAGL RWLGRVGYDP VYGARPLKRA VQRYLQDPLA EMLLEGTVTD
GMTLKVDEGD GELKMTPA
//