CLPB_DICNO
ID CLPB_DICNO Reviewed; 860 AA.
AC P17422; Q6LDM0;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB;
OS Dichelobacter nodosus (Bacteroides nodosus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2185473; DOI=10.1073/pnas.87.9.3513;
RA Gottesman S., Squires C., Pichersky E., Carrington M., Hobbs M.,
RA Mattick J.S., Dalrymple B., Kuramitsu H., Shiroza T., Foster T.,
RA Clark W.P., Ross B., Squires C.L., Maurizi M.R.;
RT "Conservation of the regulatory subunit for the Clp ATP-dependent protease
RT in prokaryotes and eukaryotes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3513-3517(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-734.
RX PubMed=1675419; DOI=10.1111/j.1365-2958.1991.tb00727.x;
RA Mattick J.S., Anderson B.J., Cox P.T., Dalrymple B.P., Bills M.M.,
RA Hobbs M., Egerton J.R.;
RT "Gene sequences and comparison of the fimbrial subunits representative of
RT Bacteroides nodosus serotypes A to I: class I and class II strains.";
RL Mol. Microbiol. 5:561-573(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 571-860.
RX PubMed=1675418; DOI=10.1111/j.1365-2958.1991.tb00726.x;
RA Hobbs M., Dalrymple B.P., Cox P.T., Livingstone S.P., Delaney S.F.,
RA Mattick J.S.;
RT "Organization of the fimbrial gene region of Bacteroides nodosus: class I
RT and class II strains.";
RL Mol. Microbiol. 5:543-560(1991).
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; M32230; AAA23344.1; -; Genomic_DNA.
DR EMBL; M32229; AAA23341.1; -; Genomic_DNA.
DR EMBL; X52390; CAA36623.1; -; Genomic_DNA.
DR EMBL; X52410; CAA36664.1; -; Genomic_DNA.
DR PIR; C35905; C35905.
DR AlphaFoldDB; P17422; -.
DR SMR; P17422; -.
DR PRIDE; P17422; -.
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; Repeat;
KW Stress response.
FT CHAIN 1..860
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191091"
FT DOMAIN 6..150
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 10..75
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 87..150
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 163..344
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 345..550
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 560..769
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 770..860
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 395..529
FT /evidence="ECO:0000250"
FT BINDING 210..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 610..617
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 860 AA; 96271 MW; 3A4EC8EB5CFC4CF1 CRC64;
MEFMQMSKKF TARFQEALSA AQSLAVGKDH AYIEPLHIFS ALLDQEGSSI IAIAQRAGGQ
IGAVRQAVMQ ALERLPRVKN PTGDVNISPE SMRLLNLCDK YAQQNGDEYI SSELFLRAVY
DAKGDLEQLL RANGLEKAAV VAAIDAVRGG EAVTDEYAED KRGALKKYTL DVTQRPLDGK
IDPVIGRDEE IRRAMQILQR RSKNNPVLIG EPGVGKTAIV EGLAQRIADR AVPESLKGKR
LLSLDLAALL AGTKYRGEFE ERLKAVLDEI TKADGQIILF IDEIHTMVGA GKSEGSLDAG
NMLKPALARG DLHCIGATTL DEYRQYMEKD AALERRFQKV IVDEPSVEDT IAILRNLQER
YEVHHGINIT DPALVAAAQL SHRYISGRKL PDKAIDLMDE AAAQIRMELD SKPEVMDKID
RRLIQLQIER MALEKETDAA SKRRLSDLEA EIAAQEKEYA DLEEIWLAEK AGNAGAAEIK
EQLDKLRVEL EAAKRRGDFA RASEIQYGLI PAKEKQLLEN EQQTEQRPHR LMRNKVTAEE
IAEIVSRWTG IPVAKMMEGE KERLLHLETV LNERVVGQKT AVEAVANAIR RNRAGLSDPK
RPIGSFLFLG PTGVGKTELC RTLAQFLFDS EENMVRIDMS EFMEKHSVAR LIGAPPGYVG
YDQGGYLTEA VRRKPYSVVL FDEVEKAHSD VFNTLLQVLD EGRLTDGQGR TVDFRHTVII
MTSNLGSDMI QLLAEKSYEE MKSAVMEIVM AHFRPEFINR IDEAIVFHGL AKTHMYRIAQ
IQLERLRQRL QTRELLLSVE EDAINQLVEL GYDPLFGARP LKRAIQNYIE NPLAQALLAG
QYLPQSTITI GFDGTNFTFH
