CLPB_BACTN
ID CLPB_BACTN Reviewed; 862 AA.
AC Q89YY3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=BT_4597;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC discriminating domain, recruiting aggregated proteins to the ClpB
CC hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC hexamer probably in an ATP-dependent manner. The movement of the
CC coiled-coil domain is essential for ClpB ability to rescue proteins
CC from an aggregated state, probably by pulling apart large aggregated
CC proteins, which are bound between the coiled-coils motifs of adjacent
CC ClpB subunits in the functional hexamer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; AE015928; AAO79702.1; -; Genomic_DNA.
DR RefSeq; NP_813508.1; NC_004663.1.
DR RefSeq; WP_008764749.1; NC_004663.1.
DR AlphaFoldDB; Q89YY3; -.
DR SMR; Q89YY3; -.
DR STRING; 226186.BT_4597; -.
DR PaxDb; Q89YY3; -.
DR PRIDE; Q89YY3; -.
DR EnsemblBacteria; AAO79702; AAO79702; BT_4597.
DR GeneID; 60925771; -.
DR KEGG; bth:BT_4597; -.
DR PATRIC; fig|226186.12.peg.4676; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_10; -.
DR InParanoid; Q89YY3; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
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; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..862
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191092"
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..71
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 81..144
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 157..338
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 339..543
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 553..770
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 771..862
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 389..520
FT /evidence="ECO:0000250"
FT BINDING 204..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 603..610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 862 AA; 97189 MW; FD5EC4B9B236D3DC CRC64;
MNFNNFTIKS QEAVQEAVNL VQSRGQQAIE PAHILHGVMK VGENVTNFIF QKLGMNGQQV
ALVVDKQIES LPKVSGGEPY LSRESNEVLQ KATQYSKEMG DEFVSLEHIL LALLTVKSTV
STILKDAGMT EKELRNAINE LRKGEKVTSQ SSEDNYQSLE KYAINLNEAA RSGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP ILIGEPGTGK TAIVEGLAHR ILRGDVPENL KNKQVYSLDM
GALVAGAKYK GEFEERLKSV VNEVKKSEGD IILFIDEIHT LVGAGKGEGA MDAANILKPA
LARGELRSIG ATTLDEYQKY FEKDKALERR FQIVQVDEPD TLSTISILRG LKERYENHHH
VRIKDDAIIA AVELSSRYIT DRFLPDKAID LMDEAAAKLR MEVDSVPEEL DEISRKIKQL
EIEREAIKRE NDKPKLEIIG KELAELKEVE KSFKAKWQSE KTLMDKIQQN KVEIENLKFE
AEKAEREGDY GKVAEIRYGK LQALDKEIED TQEKLRGMQG DKAMIKEEVD AEDIADVVSR
WTGIPVSKMM QSEKDKLLHL EDELHQRVIG QDEAIEAVAD AVRRSRAGLQ DPKRPIGSFI
FLGTTGVGKT ELAKALAEFL FDDESMMTRI DMSEYQEKHS VSRLVGAPPG YVGYDEGGQL
TEAIRRKPYS VVLFDEIEKA HPDVFNILLQ VLDDGRLTDN KGRVVNFKNT IIIMTSNMGS
SYIQSQMEKL SGSNKEEVIE ETKKEVMNML KKNIRPEFLN RIDETIMFLP LTETEIRQIV
LLQIKGVQKM LAENGVELEM TDAALNFLSQ VGYDPEFGAR PVKRAIQRYL LNDLSKKLLS
QEVDRSKAII VDSNGDGLVF RN
