ID   CLPB1_CHLTE             Reviewed;         438 AA.
AC   Q8KG79;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable chaperone protein ClpB 1;
GN   Name=clpB1; OrderedLocusNames=CT0089;
OS   Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS   (Chlorobium tepidum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=194439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX   PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA   DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA   Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA   Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA   Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA   White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA   Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT   anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(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}.
CC   -!- CAUTION: This protein is much smaller than the orthologs present in
CC       other bacteria; the N-terminal and NBD1 domains are missing. However,
CC       there is a paralog in the genome (clpB2) that encodes a protein which
CC       contains only the N-terminal and NBD1 domains. {ECO:0000305}.
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DR   EMBL; AE006470; AAM71337.1; -; Genomic_DNA.
DR   RefSeq; NP_660995.1; NC_002932.3.
DR   RefSeq; WP_010931783.1; NC_002932.3.
DR   AlphaFoldDB; Q8KG79; -.
DR   SMR; Q8KG79; -.
DR   STRING; 194439.CT0089; -.
DR   EnsemblBacteria; AAM71337; AAM71337; CT0089.
DR   KEGG; cte:CT0089; -.
DR   PATRIC; fig|194439.7.peg.89; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_9_1_10; -.
DR   OMA; FCRVDMN; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000001007; 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; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; Stress response.
FT   CHAIN           1..438
FT                   /note="Probable chaperone protein ClpB 1"
FT                   /id="PRO_0000191107"
FT   REGION          1..118
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          128..345
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          346..438
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          1..94
FT                   /evidence="ECO:0000250"
FT   BINDING         178..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   438 AA;  49655 MW;  C19CC552B2EA29FB CRC64;
     MNTADTRQRL LDIEKQIASL REEQATVKAQ WEAEKELIHT SRRLKEELED LRVQAENYER
     SGDYGKVAEI RYGKIAEIEK ALEENNRKIE ARQASGDLIM KEEIDAGDIA DIVSRWTGIP
     VSKMLQSERQ KLLGIESELH RRVVGQDEAV RAVSDAVKRS RAGMGDEKRP IGSFIFLGPT
     GVGKTELART LAEYLFDDED ALIRIDMSEY MEAHTVSRLV GAPPGYVGYE EGGQLTEAVR
     RKPFSVVLLD EIEKAHPDVF NILLQILDDG RLTDSKGRTV NFKNTIIIMT SNIGAQLIQS
     EMEHLEGRDA DAALAGLKEK LFQLLKQQVR PEFLNRIDEV ILFTPLTREN LREIVTIQFN
     RIKETARRQR ITLEISDEAL MWLAKTGFDP AFGARPLKRV MQRQITNRLS EMILAGQVGE
     DDTVEIGLEN DAIVMKKK