ID A0A173KXF8_9SPHN Unreviewed; 859 AA.
AC A0A173KXF8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=EP837_01549 {ECO:0000313|EMBL:ANI77965.1};
OS Sphingobium sp. EP60837.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1855519 {ECO:0000313|EMBL:ANI77965.1, ECO:0000313|Proteomes:UP000078304};
RN [1] {ECO:0000313|EMBL:ANI77965.1, ECO:0000313|Proteomes:UP000078304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EP60837 {ECO:0000313|EMBL:ANI77965.1,
RC ECO:0000313|Proteomes:UP000078304};
RA Lee C.-M., Yoon S.-H., Kim B.-Y.;
RT "Complete genome sequence of a organophosphorus pesticides.";
RL Submitted (JUN-2016) 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; CP015986; ANI77965.1; -; Genomic_DNA.
DR RefSeq; WP_066526088.1; NZ_CP015986.1.
DR AlphaFoldDB; A0A173KXF8; -.
DR STRING; 1855519.EP837_01549; -.
DR KEGG; sphb:EP837_01549; -.
DR PATRIC; fig|1855519.3.peg.1581; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000078304; Chromosome 1.
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:UP000078304};
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; 93592 MW; 752788ECDD8053BA CRC64;
MNLEKFTDRA KGFLQSAQTV AIRMSHQRIS PEHLLKALLE DSQGMASGLI KAAGGDPAVA
VRETDSALAK VPAVSGSGAQ QTPGLDNDAV RVLDSAEQVA AKAGDSFVTV ERLLLALTLA
TTTAAGKALA AAGVKAEGLN AAINNLRGGR TADTVGAEDR YDALKKFARD LTEAAREGKL
DPVIGRDEEI RRTIQILARR TKNNPVLIGD PGVGKTAIAE GLALRIANGD VPDTLKDRTL
MALDMGSLIA GAKYRGEFEE RLKGVLDEVK GAEGQIVLFI DEMHTLIGAG KSEGAMDAGN
LLKPALARGE LHCIGATTLD EYRKYVEKDP ALQRRFQPVF VGEPTVEDTI SILRGLKEKY
ELHHGVRITD GAIVSAATLS NRYITDRFLP DKAIDLMDEA ASRLRMEVES KPEEIENLDR
RIIQLKIERE ALKKETDKAS KDRLAALEED LANLEQQSAA LTQRWQAEKD KIAGESKLKE
QLDAARVELE QAQRAGDLAK AGELAYGRIP ELERKIAEVE GATEDAMLRE EVTSEDIASV
VSRWTGIPVD KMMEGEREKL LAMEEELGKR VIGQADAVKA VATAVRRSRA GLQDPNRPLG
SFLFLGPTGV GKTELTKALA GFLFDDDSAM VRIDMSEFME KHSVARLIGA PPGYVGYEEG
GVLTEAVRRR PYQVVLFDEV EKAHGDVFNV LLQVLDDGRL TDGQGRTVDF TNTIIVLTSN
LGSQFIASLA DDEPVEKVED QVMDIVRAHF RPEFLNRLDE VILFHRLGAS HMAPIVDIQV
GRVQKLLKDR KVVLDLTDGA RAWLGRVGYD PVYGARPLKR AVQRYLQDPL ADLILRGEVP
DGSRVKVDEG DGALQLTVG
//