ID   CLPB_MYCPA              Reviewed;         848 AA.
AC   Q73T66;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=MAP_3853;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS06403.1; -; Genomic_DNA.
DR   RefSeq; WP_003879241.1; NC_002944.2.
DR   AlphaFoldDB; Q73T66; -.
DR   SMR; Q73T66; -.
DR   STRING; 262316.MAP_3853; -.
DR   PRIDE; Q73T66; -.
DR   EnsemblBacteria; AAS06403; AAS06403; MAP_3853.
DR   KEGG; mpa:MAP_3853; -.
DR   PATRIC; fig|262316.17.peg.4102; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_11; -.
DR   OMA; SKMMQGE; -.
DR   Proteomes; UP000000580; 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   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; 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; IPR017730; Chaperonin_ClpB.
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   TIGRFAMs; TIGR03346; chaperone_ClpB; 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..848
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191143"
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          6..71
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          83..146
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          159..341
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          342..547
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          557..755
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          756..848
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          392..526
FT                   /evidence="ECO:0000250"
FT   BINDING         206..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         607..614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   848 AA;  92631 MW;  B0101B417C212A7B CRC64;
     MDSFNPTTKT QAALTAALQA ASAAGNPEIR PAHLLMALLT QADGIAAPLL EAVGVEPATI
     RAEAERMLAR LPQASGASSQ PQLSRESLAA ITTAQHLATE LDDEYVSTEH LMVGLATGDS
     DVAKLLTGHG ASPQALREAF VKVRGSARVT SPDPEATYQA LEKYSTDLTA RAREGKLDPV
     IGRDNEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVAGDVPE SLRDKTVIAL
     DLGSMVAGAK YRGEFEERLK AVLDDIKNSA GQIITFIDEL HTIVGAGATG EGAMDAGNMI
     KPMLARGELR LVGATTLDEY RKYIEKDAAL ERRFQQVFVG EPSVEDTVGI LRGLKDRYEV
     HHGVRITDSA LVAAATLSDR YITARFLPDK AIDLVDEAAS RLKMEIDSRP VEIDEVERLV
     RRLEIEEMAL AKEEDEASKE RLEKLRSELA DQKEKLAELT TRWQNEKNAI DVVRELKEQL
     ETLRGESDRA ERDGDLAKAA ELRYGRIPEV EKKLEAALPQ AEARENVMLK EEVGPDDIAE
     VVSAWTGIPA GRMLEGETAK LLRMEDELGK RVVGQKRAVQ AVSDAVRRAR AGVADPNRPT
     GSFMFLGPTG VGKTELAKAL ADFLFDDKRA MVRIDMSEYG EKHSVARLVG APPGYIGYDQ
     GGQLTEAVRR RPYTVILFDE IEKAHPDVFD VLLQVLDEGR LTDGQGRTVD FRNTILILTS
     NLGSGGSEEQ VMAAVRSAFK PEFINRLDDV IIFHGLEPGE LVQIVDIQLA QLQKRLAQRR
     LTLEVSLPAK QWLAHRGFDP VYGARPLRRL VQQAIGDQLA KQLLAGQVHD GDTVPVNVSP
     DGDSLILG