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Database: UniProt
Entry: A0A2P7QUX0_9SPHN
LinkDB: A0A2P7QUX0_9SPHN
Original site: A0A2P7QUX0_9SPHN 
ID   A0A2P7QUX0_9SPHN        Unreviewed;       867 AA.
AC   A0A2P7QUX0;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
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:PSJ41776.1};
GN   ORFNames=C7I55_05700 {ECO:0000313|EMBL:PSJ41776.1};
OS   Sphingomonas deserti.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2116704 {ECO:0000313|EMBL:PSJ41776.1, ECO:0000313|Proteomes:UP000241167};
RN   [1] {ECO:0000313|EMBL:PSJ41776.1, ECO:0000313|Proteomes:UP000241167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GL-C-18 {ECO:0000313|EMBL:PSJ41776.1,
RC   ECO:0000313|Proteomes:UP000241167};
RA   Liu L., Li L., Liang L., Zhang X., Wang T.;
RT   "The draft genome of Sphingosinicella sp. GL-C-18.";
RL   Submitted (MAR-2018) 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:PSJ41776.1}.
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DR   EMBL; PXYI01000002; PSJ41776.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P7QUX0; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000241167; 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:UP000241167};
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          415..495
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   867 AA;  94989 MW;  B67D78724C18A29F CRC64;
     MNLEKFTDRA RGFLQSAQTV AARMNHQRID PEHILKALLE DEQGMAAGLI ARAGGSAEAA
     RRETDEALAK IPTVTGSGAG SAPGLHADSI RVLDQAEQIA KKAGDSYVTV ERLLLALVLA
     ANTGAGKALA DAGVKAEALN AAINELRGGR SADTQTAEDR YDALKKFARD LTQAARDGKL
     DPVIGRDEEI RRTVQILARR TKNNPVLIGD PGVGKTAIAE GLALRIANGD VPDSLKDRKL
     MALDMGSLIA GAKYRGEFEE RLKGVLDEVK GAEGDIILFI DEMHTLIGAG KSEGAMDAGN
     LLKPALARGE LHCIGATTLD EYRKYVEKDP ALQRRFQPVF IGEPTVEDTI SILRGLKEKY
     ELHHGVRITD GALVSAATLS NRYITDRFLP DKAIDLMDEA ASRLRMEVES KPEEIETLDR
     RIIQLKIERE ALKKETDRAS KERLTALQEE LANLEQQSGE LTQRWQAEKE KIAAEGKLKE
     QLDAARLELE QAQRAGDLAK AGELQYGRIP DLEKQLAAAQ AASQSAMLRE EVTPEDIASV
     VARWTGIPME RMLEGEREKL LQMEQEIGRR VIGQADAVAA VSRAIRRSRA GLQDPNRPLG
     SFLFLGPTGV GKTELTKSLA EFLFDDPSAM VRIDMSEFME KHSVSRLIGA PPGYVGYEEG
     GVLTEAVRRR PYQVLLFDEV EKAHGDVFNI LLQVLDDGRL TDGQGRTVDF TNTIIILTSN
     LGSQYLTSLS DGQKVEEVEP QVMEVVRAHF RPEFLNRLDE IILFHRLAAE HMGPIVDIQV
     ARVQKLLADR KIRLDLTDGA RAWLGRVGYD PVYGARPLKR AVQKYLQDPL ADALLRGDVR
     DGTLVRVEEG EGGLVLGTEG PETAAAA
//
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