ID A0A3P3DY97_9RHOB Unreviewed; 872 AA.
AC A0A3P3DY97;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:RRH78412.1};
GN ORFNames=EG244_00205 {ECO:0000313|EMBL:RRH78412.1};
OS Falsigemmobacter faecalis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Falsigemmobacter.
OX NCBI_TaxID=2488730 {ECO:0000313|EMBL:RRH78412.1, ECO:0000313|Proteomes:UP000282125};
RN [1] {ECO:0000313|EMBL:RRH78412.1, ECO:0000313|Proteomes:UP000282125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 102744-1 {ECO:0000313|EMBL:RRH78412.1,
RC ECO:0000313|Proteomes:UP000282125};
RA Li G., Jiang Y.;
RT "Gemmobacter sp. nov., YIM 102744-1 draft genome.";
RL Submitted (NOV-2018) 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:RRH78412.1}.
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DR EMBL; RRAZ01000001; RRH78412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P3DY97; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000282125; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 96374 MW; D06E7770A0C0B054 CRC64;
MNLEKFTERS RGFLQAAQTI AMRETHQRLV PEHLLKALMD DDQGLSSNLI RRAGGAPERV
AESVDLTVSR LPKVSGGNGE VYTDQTLVRV LTEAEDLAKK AGDSFVPVER ILMALAMVPS
RAKEALEAGA VTAQKLNTAI NDIRKGRTAD SASAEDGYEA LKKYARDLTE AAAEGKIDPI
IGRDEEIRRT MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLRNKRLLAL
DMGSLIAGAK YRGEFEERLK SILSEVTGAA GEIILFIDEM HTLVGAGKAD GAMDAANLLK
PALARGELHC VGATTLDEYR KHVEKDAALA RRFQPVMVSE PTVEDTISIL RGIKEKYELH
HGVRIADSAL VAAATLSHRY ITDRFLPDKA IDLMDEAASR LRMEVDSKPE ELDALDRQIL
QLTIESEALK REDDAASKDR LERLEKELAD LQERSSELTA QWQAERDRLE GARELKEKLE
KARAELDIAK RDGNFAKAGE LQYGRIPELE RQIGEAEGHE SAKLVADAVR PEQIAEVIER
WTGIPTSKML EGEREKLLKM EEELGRRVIG QREAVVAVSN AVRRARAGLN DENRPLGSFL
FLGPTGVGKT ELTKAVAEYL FDDDQAMVRI DMSEFMEKHS VARLIGAPPG YVGYDEGGVL
TEAVRRRPYQ VVLFDEVEKA HPDVFNVLLQ VLDDGQLTDG QGRTVDFKQT LIILTSNLGS
QALSQLPEGS DSRLARSEVM EAVRAHFRPE FLNRLDETII FDRLTRENMD GIVEIQLRRL
QKRLEGRKIA LEVDEAGKAW LADAGYDPVF GARPLKRVIQ RYVQDPLAEL LLSGQVLDGA
VVPVSGTAEG LTIDGRLSVT PPDLLRGEKK LH
//