ID A0A5B2TBS0_9PROT Unreviewed; 856 AA.
AC A0A5B2TBS0;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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:KAA2211505.1};
GN ORFNames=F0Q34_19600 {ECO:0000313|EMBL:KAA2211505.1};
OS Pseudoroseomonas oryzae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=1608942 {ECO:0000313|EMBL:KAA2211505.1, ECO:0000313|Proteomes:UP000322110};
RN [1] {ECO:0000313|EMBL:KAA2211505.1, ECO:0000313|Proteomes:UP000322110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42542 {ECO:0000313|EMBL:KAA2211505.1,
RC ECO:0000313|Proteomes:UP000322110};
RX PubMed=26297330; DOI=.1099/ijsem.0.000449;
RA Ramaprasad E.V., Sasikala Ch., Ramana Ch.V.;
RT "Roseomonas oryzae sp. nov., isolated from paddy rhizosphere soil.";
RL Int. J. Syst. Evol. Microbiol. 65:3535-3540(2015).
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:KAA2211505.1}.
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DR EMBL; VUKA01000023; KAA2211505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B2TBS0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000322110; 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:UP000322110};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 856 AA; 93704 MW; EA0633003778C81C CRC64;
MDIEKFTERA RGFLQAAQTI AIREYHQRIT AEHLLKALLD DEQGAAAGLI RAAGADPKPV
LEAVEAELAR LPRVQGGGAG QPQFMPDIVR VLDAAQQQAG KAGDAYVAQD RLLTALAASD
TPAGRALTKA GATAQKLDGA IAAIRKGRKV DSASAEQSFD ALKKYARDLT AAAREGKLDP
VIGRDEEIRR AIQVLARRTK NNPVLIGEPG VGKTAIVEGL SLRIVNGDVP EALRNKKVLA
LDLGAMVAGA KYRGEFEERL KGVLTEVEQA AGEIVLFIDE MHTLVGAGKA DGAMDASNLL
KPALARGELH CIGATTLDEY RKHVEKDAAL ARRFQPVFVG EPSVEDTVSI LRGIKEKYEL
HHGVRIADSA LVAAAALSNR YITDRFLPDK AIDLVDEAAS RLRMQVDSKP EELDEVDRRL
LMLKIEREAL KKEDDAASRD RLTRLEREVS ELEERSDALS ASWQEEKGKL AAAQKAKEEL
DRARTEVEVA QRKGDLGRAS ELLYGVIPQL ERQIAESGDG GRLVNEAVTE EGIAAVVSRW
TGIPVDKMLE GERAKLLRME DTLRGRVVGQ EEALEAVSKA VRRARAGLQD PNRPIGSFLF
LGPTGVGKTE LTKAIAAFLF DDDKALLRID MSEYMEKHAV ARLIGAPPGY VGYEEGGALT
EAVRRRPYQV ILFDEVEKAH EDVFNVLLQV LDDGRLTDGQ GRTVDFRNTL IVLTSNLGSE
ILASQPEGED VDLVRGQVMN VVRSRFRPEF LNRLDEIVLF RRLARKDMST IVEIQLGRLR
SLLEDRKISL ELDEAALAWL AEAGYDPVYG ARPLKRVIQR NLQDQLAGML LEGRIVDGSV
VHVSADQDGL SLSVQS
//