CLPB_BIFLO
ID CLPB_BIFLO Reviewed; 889 AA.
AC Q8G4X4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=BL1250;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN25051.1; -; Genomic_DNA.
DR RefSeq; NP_696415.1; NC_004307.2.
DR RefSeq; WP_007057489.1; NC_004307.2.
DR AlphaFoldDB; Q8G4X4; -.
DR SMR; Q8G4X4; -.
DR STRING; 206672.BL1250; -.
DR PRIDE; Q8G4X4; -.
DR EnsemblBacteria; AAN25051; AAN25051; BL1250.
DR GeneID; 66506037; -.
DR KEGG; blo:BL1250; -.
DR PATRIC; fig|206672.9.peg.1535; -.
DR HOGENOM; CLU_005070_4_1_11; -.
DR OMA; SKMMQGE; -.
DR PhylomeDB; Q8G4X4; -.
DR Proteomes; UP000000439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; 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..889
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191094"
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 5..70
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 83..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 160..341
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 342..556
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 515..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..774
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 775..889
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 392..526
FT /evidence="ECO:0000250"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 616..623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 889 AA; 96314 MW; 704E8380EDA2A33C CRC64;
MEQKFTTMAQ EAVGDAIQSA SAAGNAQVET LHVMDALLRQ ENGVARSLIE AAGGDPQAIG
AAVRNALVAL PSASGSSTSQ PQASRQLTAA IAQAEKEMQQ MGDEYVSTEH LLIGIAASKP
NQSAEILEKN GVTAASLRKA VPGVRGGAKV TSPDAEGSYK ALEKYSTDLT AAAKEGKLDP
VIGRDQEIRR VIQILSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVAGDVP TTLQGKKLIS
LDLGSMVAGS KYRGEFEERL KSVLNEIKNA DGQIITFIDE IHTIVGAGAA EGSMDAGNML
KPMLARGELR LIGATTLDEY RENIEKDPAL ERRFQQVFVG EPSVEDTIAI LRGLKQRYEA
HHKVTIGDDA LVAAATLSNR YISGRQLPDK AIDLVDEAAA HLRMELDSSP EEIDELQRKV
TRLEMEEMQL KKAEDPASKE RLGKLQAELA DTREKLSGLK ARWDAEQAGH NKVGDLRAKL
DDLRVQADKY TREGNLAEAS KILYGEIPSI QKELAAAESA DAESADASAA NPADEPMVPD
RVDADSVAEI VSDWTGIPVG RLMQGENEKL LHMEDYLGKR VIGQKEAIAA VSDAVRRSRA
GISDPNRPTG SFLFLGPTGV GKTELAKALA DFLFDDEKAM VRIDMSEYME KASVSRLIGA
APGYVGYEQG GQLTEAVRRR PYSVVLFDEV EKANPEIFDV LLQVLDDGRL TDGQGRTVDF
KNTILIMTSN LGSQFLVNED MDADAKKKAV MDAVHMNFKP EFLNRLDDIV MFHPLTREEL
GGIVDIQVAG VSQRLTDRRI TLDVTDSARE WLANTGYDPA YGARPLRRLV QTEVGDQLAR
MLLAGKVHDG DTVLVDQTGG EHLELSAWAS DQIVSDNPDV SVDNVTEDK
