ID W7DJE0_9PROT Unreviewed; 868 AA.
AC W7DJE0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=COMX_09988 {ECO:0000313|EMBL:EUK17462.1};
OS Commensalibacter papalotli (ex Servin-Garciduenas et al. 2014).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1208583 {ECO:0000313|EMBL:EUK17462.1, ECO:0000313|Proteomes:UP000019250};
RN [1] {ECO:0000313|EMBL:EUK17462.1, ECO:0000313|Proteomes:UP000019250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX-MONARCH01 {ECO:0000313|Proteomes:UP000019250};
RX PubMed=24604647;
RA Servin-Garciduenas L.E., Sanchez-Quinto A., Martinez-Romero E.;
RT "Draft Genome Sequence of Commensalibacter papalotli MX01, a Symbiont
RT Identified from the Guts of Overwintering Monarch Butterflies.";
RL Genome Announc. 2:e00128-14(2014).
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:EUK17462.1}.
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DR EMBL; ATSX01000006; EUK17462.1; -; Genomic_DNA.
DR RefSeq; WP_034340928.1; NZ_ATSX01000006.1.
DR AlphaFoldDB; W7DJE0; -.
DR STRING; 1208583.COMX_09988; -.
DR PATRIC; fig|1208583.4.peg.2014; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000019250; 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:UP000019250};
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 868 AA; 95550 MW; FACCA2091F26B862 CRC64;
MNIEKFTERS QGFLQAAQTI AIREFHQQLT PQHLLKALLD DEEGAAASLI RAAGGDPKII
QGAVEHVLAS IPKVQGGGAG QPQATPELIR VLDNAEQEAT KAGDTYVAQD RLLLAIAASD
TPAGYAMQKN GVSAQNLSHA IDAIRKGRKV DTANAEASFD ALKKYARDMT EIARQGKLDP
VIGRDEEIRR AVQVLARRTK NNPVLIGEPG VGKTAIVEGL ALRIVNGDVP EALKNKQLLA
LDLGALVAGA KFRGEFEERL KAVIKEVETA AGKIILFIDE MHTIVGAGRS DGAMDASNLI
KPELARGTLH CIGATTLDEY RKYIEKDAAL ARRFQPVFVG EPSVSDTISI LRGIAEKYEL
HHGVRIADSA LVAAATLSNR YITDRFLPDK AIDLVDEAAS RLRMQIDSKP EALDELDRRL
IQLKIEREAL KREEDSASKE RLATLESEIA ALEEKSDAMT AAWHAEKEQV NAVQKLQEQL
DQARSEVEVA QRQGNLAKAS QLMYGTIPDL QKQIEDTQSK NNEHPEAGQL VSQAVTDHEI
AGVVSRWTGI PVDKMLEGER TKLLRMEDEL RERVIGQEAA LKAVSNAVRR ARAGLQDPNR
PIGSFLFLGP TGVGKTELTK ALADFLFDDE KALLRVDMSE FMEKHAVSRL IGAPPGYVGY
EEGGVLTEAV RRRPYQVILF DEVEKAHEDV FNILLQVLDD GRLTDGQGRT VDFRNTMIIL
TSNLGSDVLA NQPDGETTDM VEADVMKVVR AHFRPEFLNR LDEIILFSRL QKADMAKIVD
IQLGRLQTLL ADRKIKLNLD EKAHHWLEEA GYDPVYGARP LKRVIQRNLQ NQLAELVLQG
DVYDGEDIPV SANEKGLVIK GQQSSDLG
//