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}.
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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
//