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   18-APR-2012, entry version 52.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=MYCGA4920; ORFNames=MGA_0178;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2)).
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   MEDLINE=22830409; 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
CC       ATPase activity; ATP hydrolysis unfolds the denatured protein
CC       aggregates, which probably helps expose new hydrophobic binding
CC       sites on the surface of ClpB-bound aggregates, contributing to the
CC       solubilization and refolding of denatured protein aggregates by
CC       DnaK (By similarity).
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
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
CC       stabilizes the hexamer probably in an ATP-dependent manner. The
CC       movement of the coiled-coil domain is essential for ClpB ability
CC       to rescue proteins from an aggregated state, probably by pulling
CC       apart large aggregated proteins, which are bound between the
CC       coiled-coils motifs of adjacent ClpB subunits in the functional
CC       hexamer (By similarity).
CC   -!- SIMILARITY: Belongs to the clpA/clpB family.
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DR   EMBL; AE015450; AAP56842.1; -; Genomic_DNA.
DR   RefSeq; NP_853274.1; NC_004829.2.
DR   ProteinModelPortal; Q7NAZ3; -.
DR   SMR; Q7NAZ3; 14-197.
DR   GeneID; 1089757; -.
DR   GenomeReviews; AE015450_GR; MYCGA4920.
DR   KEGG; mga:MGA_0178; -.
DR   PATRIC; 20008835; VBIMycGal115357_0550.
DR   eggNOG; COG0542; -.
DR   HOGENOM; HBG413133; -.
DR   KO; K03695; -.
DR   OMA; KYGTLLS; -.
DR   ProtClustDB; CLSK336941; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013093; ATPase_AAA-2.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR018368; Chaperonin_ClpA/B_CS.
DR   InterPro; IPR001270; Chaprnin_ClpA/B.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 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   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Repeat; Stress response.
FT   CHAIN         1    717       Chaperone protein ClpB.
FT                                /FTId=PRO_0000191140.
FT   NP_BIND      59     66       ATP 1 (By similarity).
FT   NP_BIND     465    472       ATP 2 (By similarity).
FT   REGION       12    195       NBD1 (By similarity).
FT   REGION      196    405       Linker (By similarity).
FT   REGION      415    617       NBD2 (By similarity).
FT   REGION      618    717       C-terminal (By similarity).
FT   COILED      246    384       By similarity.
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
//