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Database: UniProt
Entry: A0A239KHF7_9SPHN
LinkDB: A0A239KHF7_9SPHN
Original site: A0A239KHF7_9SPHN 
ID   A0A239KHF7_9SPHN        Unreviewed;       858 AA.
AC   A0A239KHF7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN06295955_11448 {ECO:0000313|EMBL:SNT17420.1};
OS   Sphingopyxis indica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=436663 {ECO:0000313|EMBL:SNT17420.1, ECO:0000313|Proteomes:UP000198339};
RN   [1] {ECO:0000313|EMBL:SNT17420.1, ECO:0000313|Proteomes:UP000198339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS15 {ECO:0000313|EMBL:SNT17420.1,
RC   ECO:0000313|Proteomes:UP000198339};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZPA01000014; SNT17420.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239KHF7; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000198339; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:SNT17420.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SNT17420.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198339};
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          437..495
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   858 AA;  93331 MW;  54E69208824FD630 CRC64;
     MNLEKFTDRA KGFLQAAQTI AIRMNHQQIA PEHIAKALLE DNQGMAAGLI QRSGGDAARA
     VQGIDALLDK IPAVSGSGAQ ATPGLNNDAV RLLDQAEQVA TKAGDGYVTV ERLLLAMVLA
     SGTPVGKAFA DAGVKADALN AAINELRGGR TADTASAEDR YEALKKFARD LTEVAREGKL
     DPVIGRDEEI RRTVQILARR TKNNPVLIGE PGVGKTAIAE GLALRIANGD VPDSLKDRRL
     LALDMGALIA GAKYRGEFEE RLKGVLDDVK AAEGEIILFI DEMHTLVGAG ASEGAMDASN
     LLKPALARGE LHCIGATTLD EYRKYVEKDP ALQRRFQPVF VGEPTVEDSI SILRGLKEKY
     ELHHGVRITD GAIVAAATLS NRYITDRFLP DKAIDLMDEA ASRIRMEVES KPEEIENLDR
     RIIQMKIEES ALGKESDDAS KERLANLQAE LANLEQQSAE LTQKWQAEKD KIHAEAKIKE
     ALDAARVQLE QAQRAGDLAK AGELSYGTIP TLEKQLQEAQ AVAGNAMLRE EVTADDIAAV
     VSRWTGIPVD RMLEGEREKL LGMEAHLGQR VIGQDEAVRA VSTAVRRARA GLQDPNRPLG
     SFLFLGPTGV GKTELTKALA RFLFDDDAAM VRIDMSEFME KHSVARLIGA PPGYVGYEEG
     GVLTEAVRRR PYQVVLFDEV EKAHGDVFNI LLQVLDDGRL TDGQGRTVDF TNTLIILTSN
     LGSQAIAALP DDAPVEQAEP AVMEVVRAHF RPEFLNRLDE IVLFHRLGQQ HMGGIVDIQV
     ARVQKLLADR KITLDLTDAA RNWLGRVGYD PVYGARPLKR AVQKYLQDPL ADLILKGEVR
     DGATVKVDEG DGALTLSV
//
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