ID   CLPB_STRMU              Reviewed;         860 AA.
AC   Q8DTC7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=SMU_1425;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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 Clp repeat (R) 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; AE014133; AAN59089.1; -; Genomic_DNA.
DR   RefSeq; NP_721783.1; NC_004350.2.
DR   RefSeq; WP_002263115.1; NC_004350.2.
DR   AlphaFoldDB; Q8DTC7; -.
DR   SMR; Q8DTC7; -.
DR   STRING; 210007.SMU_1425; -.
DR   PRIDE; Q8DTC7; -.
DR   EnsemblBacteria; AAN59089; AAN59089; SMU_1425.
DR   KEGG; smu:SMU_1425; -.
DR   PATRIC; fig|210007.7.peg.1269; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_9; -.
DR   OMA; KRYITDH; -.
DR   PhylomeDB; Q8DTC7; -.
DR   Proteomes; UP000002512; 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; 1.10.1780.10; -; 1.
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; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
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; PF02861; Clp_N; 2.
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   SUPFAM; SSF81923; SSF81923; 1.
DR   PROSITE; PS51903; CLP_R; 1.
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..860
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191186"
FT   DOMAIN          2..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          5..69
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          84..148
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          161..342
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          343..543
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          553..765
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          766..860
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          393..522
FT                   /evidence="ECO:0000250"
FT   BINDING         208..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         603..610
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   860 AA;  98134 MW;  F280D52308D1372C CRC64;
     MIDKMTQLVE DSLEEAKELA IAHRNYQLDI PHLWAVLVKP DQFAFQFYQS LEINTNQLIE
     IINKEIDKIP VLSSTEKSSY ARLYSQRLKN LLDDAHQEMI DLKDQVLTVE HLILALFNQQ
     RNPITVFLLE QGLNKEKLYQ KMHRIRKGKP AISSSQETIY DALEKYAVNL NQRALDEPVN
     KIIGRQDEMN DIIRILSRKN KNNAVLVGHS GVGKTAIIEG FVQRLVKNQV PKNLQGKVIY
     SLDIGALLAG TKYRGEFEER FKALLNDIID SNGQIILFID EIHSIVSAGR TEGSVDAASI
     LKPLLARGKI RIIGSTTHAE YRESIEYDRA LERRFQRILV HEPDLDYTME ILKGLKPIYE
     NFHGVRLEED GLEAAASLSK RYISDRFLPD KALDLIDEAC AAKRLASHAY PVQMTNLSQQ
     LISEKIRLLR LTDSDTDDKF KLNNHLEQLE EQKSQLLANW QRERELLDQV QELRSHLTAL
     EEQANLALEN NQVADYVRLE DEEIRKCHQK MTALEKERLD SQKIINVTVT REDIAAVVER
     LTGIKVQGVM ENERDRLLHL EELLHQKIVG QDQAVQKVSQ AIIRSRAGIQ NPKRPIGSFL
     FLGPTGVGKT ALAKRLAEVL FGSELEMVRL DMSEYMEKHA VSRLVGPPPG YVGYEEGGQL
     TEAVRQRLYS IVLLDEIEKA HPDVFNTLLQ VLDEGRLTDS KGRTIDFKNT ILIMTSNIGS
     TNILQSLQDS GCITSEVRYK VLDELNHSFR PEFLNRIDET VLFNALSEKD MTGVVKVMVS
     DLQARLLEQD IHLTLTESVY ILLAKEGFDA AFGARPMQRT IMQKLENPLA LYLIQNQKNK
     EKETFVTVSV KDKKLKFTFS