CLPB_TREDE
ID CLPB_TREDE Reviewed; 859 AA.
AC Q73K92;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=TDE_2327;
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS12846.1; -; Genomic_DNA.
DR RefSeq; NP_972927.1; NC_002967.9.
DR RefSeq; WP_002680241.1; NC_002967.9.
DR AlphaFoldDB; Q73K92; -.
DR SMR; Q73K92; -.
DR STRING; 243275.TDE_2327; -.
DR PRIDE; Q73K92; -.
DR EnsemblBacteria; AAS12846; AAS12846; TDE_2327.
DR GeneID; 2739422; -.
DR KEGG; tde:TDE_2327; -.
DR PATRIC; fig|243275.7.peg.2196; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_12; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000008212; 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..859
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191196"
FT DOMAIN 3..146
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 83..146
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 159..340
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 341..549
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 559..766
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 767..859
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 391..525
FT /evidence="ECO:0000250"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 609..616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 859 AA; 96644 MW; B06E50D67353DFD6 CRC64;
MNIDKYTVKA SEAVQEASSL AQRDDHSQVE SEHLLYVLLE QEDGIVPPLV EKIGVSPESL
LDDLDKMLDR KPRVTGQSAQ TYISPLLAKV FANAEGYADK LKDEYVSTEH LLLALSESKD
ETGELLRSRG INLKNLLSAL KEIRGNNRVT SENPESTFRS LEKFCRDLTQ LAKNEKIDPV
IGRDEEIRRV MQVLSRRTKN NPVLIGEPGV GKTAIVEGLA RRIVSGDVPD SLKGKRLLSL
DLGALVAGAK FRGEFEERLK AVISEVQKSE GRVILFIDEL HTLVGAGASE GSMDASNLLK
PALARGELRA IGATTLNEYR KYIEKDAALE RRFQQVYCPE PTVEDTIAIL RGLQEKYEVH
HGVRIRDEAL IAAAVLSNRY ITNRFLPDKA IDLVDEAASR LKMEIESQPV ELDQVERKIL
QLNIEKVSIG KENDTASKER LLKLEEELAE LSSKRNAMQA QWQNEKARIN ESRKYKEELE
QLRIEETKYS REGNLNKAAE LKYGKIPELE KKIAAVTAEL EKKAGQQGQL LREEVCEEDI
ARIVSMWTGI PVAKMLASEM QKFLQLEKVL QARVVGQDEA VRVVSDAIRR NKAGLSDMNR
PLGSFLCIGP TGVGKTELAR TLADFLFNDE KALTRIDMSE YMEKHSVSRL IGAPPGYVGY
DEGGQLTEAV RRRPYSVILF DEIEKAHQDV FNVFLQILDD GRLTDGQGRV VDFKNTIIIM
TSNIGSEYIL TAKDMGSIKE EINQILRDNF RPEFLNRIDE ILTFNRLEKE HIRKIVDIQL
RSVAERLQAR RLGLKVSDKA KDFLADIGYD PMFGARPLKR AIQAELENKL AREVLEGKFP
EGSTILVDKG ENSLIFKKG
