GenomeNet

Database: UniProt
Entry: A0A2A2SDT6_9SPHN
LinkDB: A0A2A2SDT6_9SPHN
Original site: A0A2A2SDT6_9SPHN 
ID   A0A2A2SDT6_9SPHN        Unreviewed;       859 AA.
AC   A0A2A2SDT6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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:PAX07191.1};
GN   ORFNames=CKY28_14235 {ECO:0000313|EMBL:PAX07191.1};
OS   Sphingomonas lenta.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1141887 {ECO:0000313|EMBL:PAX07191.1, ECO:0000313|Proteomes:UP000218151};
RN   [1] {ECO:0000313|Proteomes:UP000218151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1PNM-20 {ECO:0000313|Proteomes:UP000218151};
RA   Feng G., Zhu H.;
RL   Submitted (SEP-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}.
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:PAX07191.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NSLI01000004; PAX07191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2SDT6; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000218151; 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:UP000218151};
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   859 AA;  93796 MW;  927747CE1D030D0D CRC64;
     MNLERFTDRA KGFLQSAQTV AIRMNHQRIS PEHILKALLE DEQGMAAGLI GAAGGDAKRA
     TAETDAALAK LPAVSGSGAQ TPPGLDNDAV RVLDQAEQVA QKAGDSYVTV ERMLLALTLA
     TTTAAGKALA AAGVKADALN GAINQLRGGR TADTASAEDR YDALKKFARD LTEAARDGKL
     DPVIGRDEEI RRTIQVLARR TKNNPVLIGE PGVGKTAIAE GLALRIANGD VPDGLKDKTL
     MALDMGSLIA GAKYRGEFEE RLKGVVDEVK AAEGQIILFI DEMHTLIGAG KSEGAMDASN
     LLKPALARGE LHCVGATTLD EYRKHVEKDP ALQRRFQPVF VGEPTVEDTI SILRGLKEKY
     ELHHGVRITD GAIVSATTLS NRYITDRFLP DKAIDLMDEA ASRIRMEVES KPEEIETLDR
     RIIQLKIERE ALKRENDAAS RERLAALEED LANLEQQSAE LTARWQAEKE KIGAEAKLKE
     QLDHARIELD QAQRAGDLAR AGELSYGVIP QLTRQLEEAQ AQTATAMLRE EVTADDIAAV
     VSRWTGVPVD RMLEGEREKL LRMEEVLGRR VIGQEHAVRA VSTAVRRARA GLQDPNRPLG
     SFLFLGPTGV GKTELTKALA EFLFDDANAM VRIDMSEFME KHAVARLMGA PPGYVGYEEG
     GVLTEAVRRR PYQVVLFDEV EKAHGDVFNV LLQVLDDGRL TDGQGRTVDF TNTLIILTSN
     LGSQYLANLG EGEDVESVEP QVMEVVRAHF RPEFLNRLDE VILFHRLGLA HMAPIVDIQV
     GRVAKLLGDR KIALELTDAA RAWLGRVGYD PVYGARPLKR AVQRHLQDPL AEMLLRGDVG
     DGRTVRVDEG EGKLALSVA
//
DBGET integrated database retrieval system