CLPB_MYCGE
ID CLPB_MYCGE Reviewed; 714 AA.
AC P47597;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=MG355;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L43967; AAC71580.1; -; Genomic_DNA.
DR PIR; C64239; C64239.
DR RefSeq; WP_010869446.1; NC_000908.2.
DR AlphaFoldDB; P47597; -.
DR SMR; P47597; -.
DR STRING; 243273.MG_355; -.
DR PRIDE; P47597; -.
DR EnsemblBacteria; AAC71580; AAC71580; MG_355.
DR KEGG; mge:MG_355; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_14; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR BioCyc; MGEN243273:G1GJ2-446-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; 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..714
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191141"
FT REGION 13..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..714
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 714 AA; 81039 MW; 53F58E85EB1D0ECD CRC64;
MNINFTPAGE NRNFLQEIGR NINDEVLKNK VDPIIGRDNE IRRLIEILSR KSKNNPVLIG
EPGVGKTAIV EGFVRRVVSN DVPLNLRDVE IYELSLSGLI AGTKFQGEFE KRINTILKQV
KESNGRIILF IDEIHQIVGL GRNSSSGAMD IANILKPMLA RGEIKVIGAT TLKEYREYIE
KDGALERRFQ KILINEPSSQ EALTIMRGLK TRWELFHNIT IFDSALVAAV EMSTRYINER
NLPDKAIDLI DEAAAKIKTE MSSEPVAIDS LKREIINLET EYAALKQDKE NDNKQSKKEY
LEKLKKQLDA LKQKRDSLIN EWKKEKADFE NINKLKKEIE EFQTKLETYQ SEGNYESASK
ILYSDIPRLK KELESAQQKY ATSKHDLFKT EVSENEIAEV ISQTTGIPLK KLLESEKDKL
LHLGDEIKKR VKGQDEAIDA VVNTVIRGRV NINDPNKPIG SFIFLGSTGV GKTELAKSLA
EVLFDNEKAL IRFDMSEYME KHSVAKLIGA PPGYIGYEQS GLLTEAVRRK PYSVLLFDEI
EKAHPDVTNV LLQVLDDGTL KDSQGRVVNF KNTLIIMTSN LGSNFLLEGK KDLAIQSLKK
HFRPEFINRI DEIVFFNVLE KDTVLSIINS LLAQLSKRLN KQNLFFNFDS NLTEFIYKSS
FDQQFGARPI KRFIDHSVAT LIAKYILQGK IKKGVGYNIA VVKDNITITQ NNKS
