ID   CLPB_ACICA              Reviewed;          20 AA.
AC   P82956;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   23-FEB-2022, entry version 42.
DE   RecName: Full=Chaperone protein ClpB;
DE   Flags: Fragment;
GN   Name=clpB;
OS   Acinetobacter calcoaceticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=471 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND INDUCTION.
RC   STRAIN=69-V;
RX   PubMed=11425483; DOI=10.1111/j.1574-6968.2001.tb10723.x;
RA   Benndorf D., Loffhagen N., Babel W.;
RT   "Protein synthesis patterns in Acinetobacter calcoaceticus induced by
RT   phenol and catechol show specificities of responses to chemostress.";
RL   FEMS Microbiol. Lett. 200:247-252(2001).
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   -!- INDUCTION: By heat shock, primary alcohols and monocyclic aromatics,
CC       and weakly by catechol. {ECO:0000269|PubMed:11425483}.
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   STRING; 471.BUM88_05645; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004176; Clp_R_dom.
DR   PROSITE; PS51903; CLP_R; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Nucleotide-binding; Repeat; Stress response.
FT   CHAIN           1..>20
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191083"
FT   DOMAIN          3..>20
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          6..>20
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   NON_TER         20
FT                   /evidence="ECO:0000303|PubMed:11425483"
SQ   SEQUENCE   20 AA;  2322 MW;  86BC7F082D33E5BC CRC64;
     MXFEXFTNRL QQALSDAQSL