CLPB2_CHLTE
ID CLPB2_CHLTE Reviewed; 442 AA.
AC Q8KA87;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable chaperone protein ClpB 2;
GN Name=clpB2; OrderedLocusNames=CT2281;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(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}.
CC -!- CAUTION: This protein is much smaller than the orthologs present in
CC other bacteria; the NBD2 and C-terminal domains are missing. However,
CC there is a paralog in the genome (clpB1) that encodes a protein which
CC contains only the NBD2 and C-terminal domains. {ECO:0000305}.
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DR EMBL; AE006470; AAM73494.1; -; Genomic_DNA.
DR RefSeq; NP_663152.1; NC_002932.3.
DR RefSeq; WP_010933929.1; NC_002932.3.
DR AlphaFoldDB; Q8KA87; -.
DR SMR; Q8KA87; -.
DR STRING; 194439.CT2281; -.
DR PRIDE; Q8KA87; -.
DR EnsemblBacteria; AAM73494; AAM73494; CT2281.
DR KEGG; cte:CT2281; -.
DR PATRIC; fig|194439.7.peg.2075; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_0_0_10; -.
DR OMA; EHLFIAM; -.
DR OrthoDB; 386847at2; -.
DR Proteomes; UP000001007; 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; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81923; SSF81923; 1.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..442
FT /note="Probable chaperone protein ClpB 2"
FT /id="PRO_0000191108"
FT DOMAIN 5..149
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..149
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 162..343
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 344..442
FT /note="Linker"
FT /evidence="ECO:0000250"
FT COILED 394..442
FT /evidence="ECO:0000250"
FT BINDING 209..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 442 AA; 48929 MW; BAA37E8836F1B99B CRC64;
MHFDPNKFTV KAQEALQAAS MLASSKQNQQ IEPEHLLSVM LGDHDNIACQ IARKLETPVD
TLLSVVDREI DRIPKVTGAS ATGQYISSDL GKVFDTALKE AEQLKDEYIS SEHLFIAMSE
AGVKVSKLLK DAGIDRNAIL KVLTSFRGSQ RVTSQNAEES YQSLKKYSRN LNDLVIKGKL
DPVIGRDDEI RRVLQILSRR TKNNPVLIGE PGVGKTAIVE GIAQRIVGGD VPENLKSKQI
AALDIAALVA GTKFRGEFEE RLKALVKEVQ ASDGEVILFI DELHLLVGAG SAEGSMDAAN
ILKPALARGE LRCIGATTLD EYRKHIEKDA ALERRFQTVI VDQPSVEDTV SILRGLKEKY
EIHHGVRIKD AALVAAAELS NRYIADRFLP DKAIDLIDEA CSRLRLEIDS EPEELDRINR
ELRRLEIERE ALKRELEATG SV
