CLPB_MYCTO
ID CLPB_MYCTO Reviewed; 848 AA.
AC P9WPD0; L0T577; O53719; P63288;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=MT0397;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(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; AE000516; AAK44619.1; -; Genomic_DNA.
DR PIR; C70834; C70834.
DR RefSeq; WP_003401905.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPD0; -.
DR SMR; P9WPD0; -.
DR PRIDE; P9WPD0; -.
DR EnsemblBacteria; AAK44619; AAK44619; MT0397.
DR KEGG; mtc:MT0397; -.
DR PATRIC; fig|83331.31.peg.423; -.
DR HOGENOM; CLU_005070_4_2_11; -.
DR Proteomes; UP000001020; 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; Repeat;
KW Stress response.
FT CHAIN 1..848
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000426973"
FT DOMAIN 1..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..341
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 342..547
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 557..755
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 756..848
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 392..524
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 607..614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 848 AA; 92568 MW; 41CE8DFA9D5EBAC9 CRC64;
MDSFNPTTKT QAALTAALQA ASTAGNPEIR PAHLLMALLT QNDGIAAPLL EAVGVEPATV
RAETQRLLDR LPQATGASTQ PQLSRESLAA ITTAQQLATE LDDEYVSTEH VMVGLATGDS
DVAKLLTGHG ASPQALREAF VKVRGSARVT SPEPEATYQA LQKYSTDLTA RAREGKLDPV
IGRDNEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVAGDVPE SLRDKTIVAL
DLGSMVAGSK YRGEFEERLK AVLDDIKNSA GQIITFIDEL HTIVGAGATG EGAMDAGNMI
KPMLARGELR LVGATTLDEY RKHIEKDAAL ERRFQQVYVG EPSVEDTIGI LRGLKDRYEV
HHGVRITDSA LVAAATLSDR YITARFLPDK AIDLVDEAAS RLRMEIDSRP VEIDEVERLV
RRLEIEEMAL SKEEDEASAE RLAKLRSELA DQKEKLAELT TRWQNEKNAI EIVRDLKEQL
EALRGESERA ERDGDLAKAA ELRYGRIPEV EKKLDAALPQ AQAREQVMLK EEVGPDDIAD
VVSAWTGIPA GRLLEGETAK LLRMEDELGK RVIGQKAAVT AVSDAVRRSR AGVSDPNRPT
GAFMFLGPTG VGKTELAKAL ADFLFDDERA MVRIDMSEYG EKHTVARLIG APPGYVGYEA
GGQLTEAVRR RPYTVVLFDE IEKAHPDVFD VLLQVLDEGR LTDGHGRTVD FRNTILILTS
NLGSGGSAEQ VLAAVRATFK PEFINRLDDV LIFEGLNPEE LVRIVDIQLA QLGKRLAQRR
LQLQVSLPAK RWLAQRGFDP VYGARPLRRL VQQAIGDQLA KMLLAGQVHD GDTVPVNVSP
DADSLILG
