CLPB_MYCLE
ID CLPB_MYCLE Reviewed; 848 AA.
AC Q9CB26;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=ML2490;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL583925; CAC32007.1; -; Genomic_DNA.
DR PIR; G87220; G87220.
DR RefSeq; NP_302608.1; NC_002677.1.
DR RefSeq; WP_010908927.1; NC_002677.1.
DR AlphaFoldDB; Q9CB26; -.
DR SMR; Q9CB26; -.
DR STRING; 272631.ML2490; -.
DR PRIDE; Q9CB26; -.
DR EnsemblBacteria; CAC32007; CAC32007; CAC32007.
DR KEGG; mle:ML2490; -.
DR PATRIC; fig|272631.5.peg.4782; -.
DR Leproma; ML2490; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_11; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000000806; 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..848
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191142"
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; 93207 MW; 66BE8AF060DCEC96 CRC64;
MDSFNPTTKM QVALTSALQA ASSAGNPEIR PVHLLLAMLM QNDGIAAPLL ETVGVEPDIV
RNEAQRLLER LPQASGCSSQ PQLSRESLAA ITTAQQLATE MDDEYVSTEH LMLGLAMGDS
DVAKLLTGHG ASPQVLREAF VKIRGSARVT SSDPEFTYQA LEKYSTDLTA QSGEGKLDPV
IGRDNEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVAGDVPE SLRDKTLVAL
DLGSMVAGAK YRGEFEQRLK VVLDDIKFSA GQIITFIDEL HTIVGAGATG ESAMDAGNMI
KPMLARGELR LVGATTLDEY RRYIEKDAAL ERRFQQIFVG EPSVEDTVGI LRGLKDRYEV
HHGVRITDSA LVAAAALSDR YITARFLPDK AIDLVDEAAS RLRMEIDSRP VEIDEVERLV
RRFEIEEMAL VNEEDEASKE RLETLRAELA DQKERLAELT ARWQNEKNAI DVVRELKEQL
ETLRGESERA ERDGDLAKAA ELRYGRIPEV EKKLEAAVPT AQAREDVMLK EEVGPDDIAN
VVSAWTGIPA GRLLEGETAK LLRMEDELGK RVVGQKKAVH AVSDAVRRSR AGVADPNRPT
GSFLFLGPTG VGKTELAKAL ADFLFDDQRA MVRVDMSEYG EKHSVARLVG APPGYIGHDQ
GGQLTEAVRR RPYTVVLFDE VEKAHSDVFD VLLQVLDEGR LTDGQGRTVD FRNTIPILTS
NLGSGGSEEQ VMAAVRSVFK PEFINRLDDV LIFDGLNPEE LVRIVDIQLE QLGKRLAQRR
LQLEVSLPAK RWLAQHGFDP VYGARPLRRL VQQAIGDQLA KMLLAGEVHD GDTLPVNVRP
DGEALILG
