CLPB2_THEVB
ID CLPB2_THEVB Reviewed; 887 AA.
AC Q8DG71;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Chaperone protein ClpB 2;
GN Name=clpB2; OrderedLocusNames=tll2453;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(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}.
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DR EMBL; BA000039; BAC10004.1; -; Genomic_DNA.
DR RefSeq; NP_683242.1; NC_004113.1.
DR RefSeq; WP_011058284.1; NC_004113.1.
DR AlphaFoldDB; Q8DG71; -.
DR SMR; Q8DG71; -.
DR STRING; 197221.22296180; -.
DR PRIDE; Q8DG71; -.
DR EnsemblBacteria; BAC10004; BAC10004; BAC10004.
DR KEGG; tel:tll2453; -.
DR PATRIC; fig|197221.4.peg.2577; -.
DR eggNOG; COG0542; Bacteria.
DR OMA; GPEHILM; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000000440; 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..887
FT /note="Chaperone protein ClpB 2"
FT /id="PRO_0000191188"
FT DOMAIN 6..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 9..73
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 84..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 160..342
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 343..559
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 569..780
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 781..887
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 393..535
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 619..626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 887 AA; 99840 MW; DEFBD65AD7500674 CRC64;
MQPTDPTKFT DKAWEAIVKS QDVAREYRSQ YLETEHVMIA LLREEGLGQV ILERSDIDTE
WVLKRLMDFA RQQPRVPAGS ELYCGRSLDA LLDEANRLRQ EEEDQFISIE HLLLAFVGDR
RIGQRLFRAL NCDRQQLAAT VKAIRGAQKV LDQNPENKYA ALEKYGRDLT EAARQGKLDP
VIGRDEEIRR VIQVLSRRTK NNPVLIGEPG VGKTAIAEGL AQRIINGDVP ESLKNRRLIS
LDLGSLVAGA KFRGDFEDRL KAVLHEVTHS EGQIVLFIDE LHTVVGAGAN QNSSMDASNL
LKPMLARGEL RCIGATTLDE YRKYIEKDAA LERRFQQVYI GQPSVEDTIS ILRGLKDRYE
IHHNVKITDS ALVAAAMLSD RYISDRYLPD KAIDLVDEAA AKLKMEITTK PAELEALERR
LRQLEMERLS LKQEESLPLS QAPLQATRDR LQRIEAEIAQ LQPRQQAMQA RWQAEKELLE
RINSLKEEED QVKLQIEQAE RDYNLNKAAQ LKYGRLETLQ RELEATEAQL LELQAAGGTF
LRDQVTEADI AEIVAKWTGI PLQKLMASER QKLLQLEQVL HQRVIGQSDA VAAVAAAIRR
ARAGMKDPAR PIGSFLFMGP TGVGKTELAR ALAEALFDDE NALVRIDMSE YMEKHAVSRM
IGAPPGYVGF DSGGQLTEAI RRRPYAVVLF DEVEKAHPEV FNVLLQVLDD GRITDSQGRT
VDFRNTVIIM TSNLGSEHIL DLAADDSRYE EMRQRVLQSA QKYFRPEFLN RIDDVILFHG
LGRTELAQIA QIQLRRVEKL LADQKIHLRL TPAALDHLVA VGFDPVYGAR PLKRAIQREL
ENPLAVKLLE EVFTPGDTIL VDLVGSELTF RAVSPAGTGD RDTVSAS
