ID CLPB_MYCPN Reviewed; 715 AA.
AC P75247;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=MPN_531; ORFNames=MP311;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS (Mycoplasmoides pneumoniae).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129 / Subtype 1;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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 N-terminal 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; U00089; AAB95959.1; -; Genomic_DNA.
DR PIR; S73637; S73637.
DR RefSeq; NP_110220.1; NC_000912.1.
DR RefSeq; WP_010874888.1; NZ_OU342337.1.
DR AlphaFoldDB; P75247; -.
DR SMR; P75247; -.
DR IntAct; P75247; 1.
DR STRING; 272634.MPN_531; -.
DR EnsemblBacteria; AAB95959; AAB95959; MPN_531.
DR KEGG; mpn:MPN_531; -.
DR PATRIC; fig|272634.6.peg.592; -.
DR HOGENOM; CLU_005070_4_0_14; -.
DR OrthoDB; 9803641at2; -.
DR BioCyc; MPNE272634:G1GJ3-876-MONOMER; -.
DR Proteomes; UP000000808; 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 CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
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 PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 2.
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..715
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191145"
FT REGION 14..196
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 197..406
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 416..618
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 619..715
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 247..385
FT /evidence="ECO:0000250"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 466..473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 715 AA; 81396 MW; 1F1C69E51201FDE2 CRC64;
MDFSFTPTPD KRDFLKEMGR SINDEVLKNK VDPIIGRDNE IRRLIEILSR KNKNNPVLIG
EPGVGKTAIV EGFVRRVVNN DVPLNLRDVE IYELSLSGLI AGTQYQGEFE KRVNGILKQV
KESNGKIILF IDEIHQIVGL GRNSSSGAMD IANILKPMLA RGEIKVIGAT TLKEYREYVE
KDGALERRFQ KILVSEPSQQ EALTIMRGLK TRWELFHNLT IFDSALVAAV EMSARYIPDR
NLPDKAIDLI DEASAKIKTE MASEPVVIDT LKREIINLET EYAALKQDKE NADNKKKQGH
LDNLKQQLDE LKKKRDSLTA EWKKEKTNFE SINKLKKEIE DLQTRLELYQ TEGNYEAASK
ILYYDIPKLK NQLEQAQKKY VDSKHDLFKT EVSENEVAEV VSQATGIPLK KLLETEKEKL
LHLGDEIKKR VKGQDAAVET VVNTVMRGRV NLNDPNRPIG SFIFLGSTGV GKTELAKSLA
EVLFDNEKAM IRFDMSEYME KHSVAKLIGA PPGYVGYEQS GLLTEAVRRK PYCVLLFDEI
EKAHPDVTNI LLQVLDDGTL KDSQGRLVNF KNTMIIMTSN LGSNYIMENK RDLAMEALKK
HFRAEFINRI DEIVFFSVLQ KTTVLEIITN LLDQLNQRLA KQNLKFTFDP KLNEFIYKSS
FDEQFGARPI KRFIDRQIAT LIAKQILEGI ITKDVSYNVI VEKDKVAIVA NKVKS
//
