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Database: UniProt
Entry: A0A547P9F9_9SPHN
LinkDB: A0A547P9F9_9SPHN
Original site: A0A547P9F9_9SPHN 
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
//
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