ID A0A5C4MQN4_9RHOB Unreviewed; 874 AA.
AC A0A5C4MQN4;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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:TNC47871.1};
GN ORFNames=FHG66_15475 {ECO:0000313|EMBL:TNC47871.1};
OS Rubellimicrobium rubrum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=2585369 {ECO:0000313|EMBL:TNC47871.1, ECO:0000313|Proteomes:UP000305887};
RN [1] {ECO:0000313|EMBL:TNC47871.1, ECO:0000313|Proteomes:UP000305887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 131921 {ECO:0000313|EMBL:TNC47871.1,
RC ECO:0000313|Proteomes:UP000305887};
RA Jiang L.;
RT "YIM 131921 draft genome.";
RL Submitted (JUN-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:TNC47871.1}.
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DR EMBL; VDFU01000021; TNC47871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C4MQN4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000305887; 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};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000305887};
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 REGION 431..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 874 AA; 96432 MW; ACC71BDEC2595DA3 CRC64;
MNLEKFTERS RGFLQAAQTI AIREQNQRVL PEHLLKALMD DDQGLAANLI DRSGGSSARV
REAVDAAVAR QPKVSGDAGQ AYVDSSLVRV LDEAEKVATK AGDSFVPVER MLMALAMVKS
KAQEALDAGA VTAQKLNAAI NDVRKGRTAD TASAEEGYDA LRKYARDLTE AARDGKIDPI
IGRDEEIRRS MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVNGDVPE SLRNKTLMAL
DMGSLIAGAK YRGEFEERLK AVLKEIEAAA GEVIVFIDEM HTLVGAGKAD GAMDAANLIK
PALARGELHC IGATTLDEYR KHVEKDAALA RRFQPIMVEE PTVEDTISIL RGIKEKYELH
HGVRISDSAL VAAAQLSHRY ITDRFLPDKA IDLVDEAASR LRMEIDSKPE ELDQLDRQLL
QLQIEAEALK KEDDDASKDR LSRLEKEMSE VQERSAAMTA KWQAERATLE SARFVKERLE
DARAQLDRAK REGNLAEAGR LAYGEIPQLE RELAEAETQG DGLMVEEAVR PEQIAEVVER
WTGIPTSRML EGERDKLLRM EEALGKRVVG QRAAVEAVSR AVRRARAGLN DEGRPLGSFL
FLGPTGVGKT ELTKALAEFL FDDDTAMVRI DMSEFMEKHA VSRLIGAPPG YVGYDEGGVL
TEAVRRRPYQ VVLFDEVEKA HPDVFNVLLQ VLDDGMLTDG QGRTVDFKQT IIVLTSNLGA
RALSELPEGS DATLAKREVM EAVRTHFRPE FLNRLDEQII FDRLDRSDMT GIVEIQLKRL
EKRLAARKIR LDLDQGAKQW LADEGYDPVF GARPLKRVIQ RALQDQLAEM ILAGEVRDDE
TVTVTAGPDG LIVGNRVASG SGARTDRPMD AVVH
//