CLPB_CLOPE
ID CLPB_CLOPE Reviewed; 866 AA.
AC Q8XKG8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=CPE1428;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(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; BA000016; BAB81134.1; -; Genomic_DNA.
DR RefSeq; WP_011010440.1; NC_003366.1.
DR AlphaFoldDB; Q8XKG8; -.
DR SMR; Q8XKG8; -.
DR STRING; 195102.gene:10490692; -.
DR EnsemblBacteria; BAB81134; BAB81134; BAB81134.
DR KEGG; cpe:CPE1428; -.
DR HOGENOM; CLU_005070_4_2_9; -.
DR OMA; GPEHILM; -.
DR Proteomes; UP000000818; 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..866
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191112"
FT DOMAIN 3..151
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 86..151
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 164..345
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 346..552
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 562..773
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 774..866
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 396..530
FT /evidence="ECO:0000250"
FT BINDING 211..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 612..619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 866 AA; 97939 MW; 4EB48CEFBB16DB8B CRC64;
MNADKMTLRV QQSLNDAYEI AVKYNNQQLD IIHLFSALVN QKDGLIPNIF EKMGVNIDSL
KRDIHVQIDR MPKVLGEAAQ SSGVTATRRI NEVLIKAEEI SKQFEDSYIS VEHVMLAMID
IDKNGAVGEI LRKNNITKDG FLKVLNEVRG SQRVDSQDPE GTYEALDKYG TNLIELVKQH
KLDPVIGRDE EIRRAVRILS RKTKNNPILI GEPGVGKTAI VEGLAERIVR GDVPEGLKDK
VIISLDMGAL IAGAKYRGEF EERLKAVLKE VQSSEGKILL FIDEIHTIVG AGKTDGAMDA
GNLIKPMLAR GELHCIGATT FDEYRQYIEK DKALERRFQP VIVEEPTVEE TVSILRGLKE
RFEIHHGIRI HDSAIVAAAK LSHRYIQDRY LPDKAIDLID EAGAMIRSEI DSLPTELDII
RRKILMLETE KEALSKENDD ASKERLVALE KELAELQDKN DEMTIKYEKE KSHISAVRDL
KAELDEARGL AEKYEREYDL NKVAELKYGK IPELERKIKE QEASMEKDNE NALLKEEVTE
NEISEIISKW TGIPVTKLVE SEREKLLRLE EELRERVIGQ DEATTAVANA VIRARAGLKD
ERKPIGSFIF LGPTGVGKTE LAKTLARNLF DSEDNIVRID MSEYMEKHAV SRLIGPPPGY
VGYEEGGQLT EAVRRNPYSV ILFDEIEKAH DDVFNLFLQI LDDGRLTDNK GKTVDFKNTI
IIMTSNIGSG YLLENKSGEG IEDDIRENVM NEMKLRFKPE FLNRVDDIIM FRPLSSEGIK
KIIDIFLRDV ENRLRERNIT LEVTDRAKEI LAEEGYDPVY GARPLKRYIS NVLETEIAKK
IIAGEIYDGS VALIDGVDGK IIVSRK
