ID A0A5C6UKE9_9SPHN Unreviewed; 859 AA.
AC A0A5C6UKE9;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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:TXC73552.1};
GN ORFNames=FSZ31_02045 {ECO:0000313|EMBL:TXC73552.1};
OS Sphingorhabdus soli.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingorhabdus.
OX NCBI_TaxID=2601267 {ECO:0000313|EMBL:TXC73552.1, ECO:0000313|Proteomes:UP000321129};
RN [1] {ECO:0000313|EMBL:TXC73552.1, ECO:0000313|Proteomes:UP000321129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D-2Q-5-6 {ECO:0000313|EMBL:TXC73552.1,
RC ECO:0000313|Proteomes:UP000321129};
RA Liu Y.;
RT "Sphingorhabdus soil sp. nov., isolated from arctic soil.";
RL Submitted (AUG-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:TXC73552.1}.
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DR EMBL; VOPY01000001; TXC73552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C6UKE9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000321129; 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:UP000321129};
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; 93807 MW; C79DD61BFB647CDF CRC64;
MNLEKFTDRA KGFLQSAQTV AIRMNHQRIS PEHLLKALLE DNEGMAAGLI ARAGGDPKVA
VTAVDAALAK VPAVSGSGAQ QTPGLDNDTV RVLDQAEQVA DKAGDSYVTV ERLLLALTLA
KTTTAGKALA DARLTPEALN SAINELRGGR TADTASAEDR YDALKKFARD LTQAARDGEL
DPVIGRDEEI RRTIQILARR TKNNPVLIGE PGVGKTAIAE GLALRIVNGD VPDTLKDRTL
MALDMGSLIA GAKYRGEFEE RLKGVLDEVK GADGQIVLFI DEMHTLIGAG KSEGSMDASN
LLKPALARGD LHCIGATTLD EYRKHVEKDP ALQRRFQPVF IGEPTVEDTI SILRGLKEKY
ELHHGIRITD GALVSAATLS HRYISDRFLP DKAIDLMDEA ASRIRMEVES KPEEIEALDR
RIIQLKIERE ALKKETDKPS QDRLASLEDE LANLEQQSSE LTARWKGEKD KIHAESRLKE
QLDAARIELD QAQRGGDLAK AGELSYGTIP ELERKLADAG VASEGAMLRE EVTADDIAGV
VSRWTGIPVD RMMEGEREKL LGMEAAIGKR VIGQAEAVKA VATAVRRSRA GLQDPNRPLG
SFLMLGPTGV GKTELTKALA GFLFDDDSAM VRIDMSEFME KHAVARLIGA PPGYVGYEEG
GVLTEAVRRR PYQVVLFDEV EKAHGDVFNI LLQVLDDGRL TDGQGRTVDF SNTLIILTSN
LGSQYLTGLK DGEDVESVEP QVMEVVRAHF RPEFLNRLDE IILFHRLAQE HMAGIVDIQV
GRVQKLLADR KVTLDLTEAA RAWLGRVGYD PVYGARPLKR AVQKYVQDPL ADMILRGEVP
DGSTIKVDEG DGALELKVS
//