ID   CLPB_CAMJE              Reviewed;         857 AA.
AC   Q9PI02; Q0PB06;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=Cj0509c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(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; AL111168; CAL34656.1; -; Genomic_DNA.
DR   PIR; F81396; F81396.
DR   RefSeq; WP_002858618.1; NC_002163.1.
DR   RefSeq; YP_002343941.1; NC_002163.1.
DR   AlphaFoldDB; Q9PI02; -.
DR   SMR; Q9PI02; -.
DR   IntAct; Q9PI02; 1.
DR   STRING; 192222.Cj0509c; -.
DR   PaxDb; Q9PI02; -.
DR   PRIDE; Q9PI02; -.
DR   EnsemblBacteria; CAL34656; CAL34656; Cj0509c.
DR   GeneID; 904838; -.
DR   KEGG; cje:Cj0509c; -.
DR   PATRIC; fig|192222.6.peg.502; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_7; -.
DR   OMA; ERMKAVM; -.
DR   Proteomes; UP000000799; 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..857
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191101"
FT   DOMAIN          4..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          8..73
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          86..147
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          160..340
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          341..548
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          558..764
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          765..857
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          391..525
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         608..615
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   857 AA;  95544 MW;  ADED298D0B293073 CRC64;
     MANIQDFLTD NMLSNLESAA SLAIHSKNNE VVPLHLLWAL SVDSTSILNQ ILNKLNISKE
     ALELEIKSRI SKLATSSNVN RENIRFSNEL INSLENAKGL MSANGDSYLS VDTWLISESQ
     KSPIKEILAQ FLDLREFQKE LESLRAGRKM DSKTSDETLD SLNKFGIDLT LKASEGKLDP
     VIGREEEIER LMQILIRKTK NNPILLGEPG VGKTAIVEAL AQRIIKKDVP KSLQNKKVIA
     LDMSALIAGA KYRGEFEDRL KAVVNEVIKS ENIILFIDEI HTIVGAGASE GSMDAANILK
     PALARGELHT IGATTLKEYR KYFEKDAALQ RRFQPVNVGE PSVNEALAML RGIKEKLEIH
     HNVTINDSAL VAAAKLSKRY IADRFLPDKA IDLIDEAAAE LKMQIESEPS SLRKVRKDIE
     TLEVENEALK MENDEKNQKR LDEIAKELAN LKEKQNALNS QFENEKSVFD GISAKKKEID
     LLKNEASLAK ARGEFQKAAE LEYGKIPSLE KEVEILEDKW KKMSENGVLL KNQVDEDLVA
     GILSKWTGIS VQKMLTSEKQ KFLEVEKHLK ESVIGQDKAL SALARAIKRN KAGLNADNKP
     IGSFLFLGPT GVGKTQSAKA LAKFLFDDEK AMIRFDMSEF MEKHSVSRLL GAPPGYIGHE
     EGGELTEAVR RKPYSVLLFD EVEKAHKDVF NVLLGILDDG RATDSKGVTV DFKNTIIILT
     SNIASNAIMN LSGKEQEDAV KNELKNFFKP EFLNRLDDII TFNPLGKDEA YEIVKLLFKD
     LQMSLENKGI KASLSENAAL LIAKDGFDPD FGARPLRRAI YDLIEDKLSD MILADELHEN
     DSIIIDAKDD EIIIKKA