ID   CLPB_RHILO              Reviewed;         868 AA.
AC   Q98G96;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=mll3429;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB50320.1; -; Genomic_DNA.
DR   RefSeq; WP_010911666.1; NC_002678.2.
DR   AlphaFoldDB; Q98G96; -.
DR   SMR; Q98G96; -.
DR   STRING; 266835.14023715; -.
DR   PRIDE; Q98G96; -.
DR   EnsemblBacteria; BAB50320; BAB50320; BAB50320.
DR   KEGG; mlo:mll3429; -.
DR   PATRIC; fig|266835.9.peg.2730; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_5; -.
DR   OMA; ERMKAVM; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000000552; 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; Repeat;
KW   Stress response.
FT   CHAIN           1..868
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191165"
FT   DOMAIN          3..147
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..147
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          160..341
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          342..545
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          555..765
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          766..868
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          392..523
FT                   /evidence="ECO:0000250"
FT   BINDING         207..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         605..612
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   868 AA;  95979 MW;  5EAF32DBB48A184C CRC64;
     MNLEKYSERV RGFIQSAQTM ALSRNHQQFT PEHILKVLVD DDEGLAASLI ERAGGNVRDV
     KLGVETALEA MPKVEGGNGQ LYLAQPLAKV FSTAEELAKK AGDSFVTVER LLQALTMEKS
     AKTADILAKA GVTAQALNQV INDVRKGRTA DSASAEQNYD ALKKYARDLT ADARAGKLDP
     VIGRDDEIRR TIQVLSRRTK NNPVLIGEPG VGKTAIAEGL ALRIVNGDVP ESLKDKQLMA
     LDMGALIAGA KYRGEFEERL KAVLSEVTSA NGNIILFIDE MHTLVGAGKA DGAMDASNLL
     KPALARGELH CVGATTLDEY RKHVEKDPAL ARRFQPVFVD EPTVEDTVSI LRGLKEKYEQ
     HHKVRISDSA LVAAATLSNR YIADRFLPDK AIDLVDEAAS RLRMQVDSKP EALDEIDRRI
     MQLKIEREAL KVETDDASKD RLVRLEKELV GLEEESTEIT AKWQAEKQKL GLAADLKKQL
     DEARNELAIA QRKGEFQRAG ELAYGKIPEL EKKLKEAEAQ DGKAGMVEEV VTPDHVAHIV
     SRWTGIPVDK MLQGERDKLL RMEDEIGKRV VGQGEAVQAV SKAVRRARAG LQDPNRPIGS
     FIFLGPTGVG KTELTKALAS FLFDDDSAMV RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
     ALTEAVRRRP YQVVLFDEIE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NTLIIMTSNL
     GAEYLVNLGE DQDVDAVRDE VMGVVRASFR PEFLNRVDEV ILFHRLRRKD MDRIVEIQFK
     RLESLLVDRK ITLSLDHEAI EWLAAKGYDP AYGARPLKRV MQKELQDPLA EKILLGEILD
     GSTVKVTSGS DRLNFRSKPT VVATEAAA