ID   CLPB_MALP2              Reviewed;         705 AA.
AC   Q8EW28;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=MYPE3790;
OS   Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC   Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX   NCBI_TaxID=272633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF-2;
RX   PubMed=12466555; DOI=10.1093/nar/gkf667;
RA   Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA   Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT   "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT   bacterial pathogen in humans.";
RL   Nucleic Acids Res. 30:5293-5300(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 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; BA000026; BAC44168.1; -; Genomic_DNA.
DR   RefSeq; WP_011077204.1; NC_004432.1.
DR   AlphaFoldDB; Q8EW28; -.
DR   SMR; Q8EW28; -.
DR   STRING; 272633.26453837; -.
DR   PRIDE; Q8EW28; -.
DR   EnsemblBacteria; BAC44168; BAC44168; BAC44168.
DR   KEGG; mpe:MYPE3790; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_14; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000002522; 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   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..705
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191144"
FT   REGION          12..195
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          196..399
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          409..611
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          612..705
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          246..378
FT                   /evidence="ECO:0000250"
FT   BINDING         59..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         459..466
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   705 AA;  80957 MW;  8BC03933B832D803 CRC64;
     MEFNFEPSNE KDILKKYSRN LNEEVSANKL NKIIGREQEI RRVIEILSRK EKNNPVLIGE
     PGVGKTAIVE GFVQKIISKE VPENLVHCVV YEVNLSSLIA GTFLQGEFEK RLNALIKEAK
     QNNGAVILFI DEIHQLMGMG KAGNNSGMDA ANILKPIMAR GEIKIIGATT SNEYRQYIEK
     DGALERRFQK ILVEEPTPEE ALTIMRGLKE KWEIYHKVRI QDNALVASVK LSERYISDKY
     LPDKAIDLID EAAAKIKTEA HTSPSEPINK KIFYLETEKI ALSKEEGTNQ KERINEIEIE
     LEKLKQERDL VEKEWKEQKE QQVALNKIKK EIEKNNWDVE RYQNQGEYTE ASKILYSVLP
     ELKKKLEAIE KSISENKKVL IKDYISEIDV AEIISRITKI PLNKIFEKEQ DKLLNLFNNL
     KKRVKGQDEA LKLVSDTVLK NRVGINNPNR PIGSFLFVGP TGVGKTEVAK SLAENLFNTE
     KAIVRINMSE YMEKHSISRL IGAPPGYIGY EQAGELSEQI RRKPYSVVLL DEIEKAHPDI
     LNVLLQVLDE GTLKDNQGRN INFKNTIIIM TSNVGALYLM ENKEDMFERE LKTSFKPEFL
     NRIDEIIKFN SITMEFAKEI AQKMLDDLEK RLKDNNYQIT FDKSVVEYVA KNGYSKEYGA
     RPINRFIQKT IENFITESIL KNELIKDRST IINFANNKLA ILKSN