ID   CLPB_MYCGA              Reviewed;         717 AA.
AC   Q7NAZ3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=MYCGA4920; ORFNames=MGA_0178;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
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; AE015450; AAP56842.1; -; Genomic_DNA.
DR   RefSeq; WP_011113741.1; NC_004829.2.
DR   AlphaFoldDB; Q7NAZ3; -.
DR   SMR; Q7NAZ3; -.
DR   PRIDE; Q7NAZ3; -.
DR   KEGG; mga:MGA_0178; -.
DR   PATRIC; fig|233150.7.peg.550; -.
DR   HOGENOM; CLU_005070_4_0_14; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000001418; 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..717
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191140"
FT   REGION          12..195
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          196..405
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          415..617
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          618..717
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          246..384
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         465..472
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   717 AA;  81402 MW;  407BD89660ADE13A CRC64;
     MFASFTPTEE KNVLSKYSRN LNDEIARNAI DPTIGREEEI RRLIEILSRK NKNNPVLIGE
     PGVGKTAIVE GFARKIVNGD VPDNLKDVEV VELSLSSLIA GTQFQGSFEE RLNKILKEVK
     NSSGKVILFI DEIHQLVGMG KNSSNSAMDA ANILKPMMAR GEIKVIGATT IDEYRKYIEK
     DGALERRMQK ILVDEPTKQE ALTIMRGLRE RWEAFHKVRI FDDALVAAVE MSARYISDRY
     LPDKAIDLID EAAAKIKTLI HSLPPELDNI KQKIIHLSTE LAALEREKKE NHSNVRLGRI
     EQLKKEIKDF TNKQNELTVK WTQQKTIYEC INKLKEEVTN LTAEIERLQA KGEYTQASKL
     LYLEIPKRQE EIEKKTKELS EFTDNLIKTS ISRVEIAEVI SQATKIPLSK LVASEQQKLL
     NLKNDLSKYI KGQDHAIKNV SDAVLRGRAQ INDPNRPIGS FLFLGPTGVG KTEVAKKLAY
     CLFDNEKAMV RIDMSEFMER HSVDKLIGSP PGYIGYDQPG VLSDAIRTKP YAVVLFDEIE
     KAHPDVLNIL LQILDDGQLT DNHNRLVNFK NTIIIMTSNI GAEHILANNP AKTIEELKRK
     IRPELLNRID ELITFKALND KDLSAIAQKL LSDLSDRIKK QQINITFDKK IVENVVKHGS
     NTVFGARPLK RYIQREVENF LAKKIIENKL EKNKSYVCTF NAETNEYTLV NLRKAVS