CLPB2_SYNE7
ID CLPB2_SYNE7 Reviewed; 895 AA.
AC O34209; Q31QK0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Chaperone protein ClpB 2;
GN Name=clpB2; OrderedLocusNames=Synpcc7942_0637;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11717299; DOI=10.1128/jb.183.24.7392-7396.2001;
RA Eriksson M.J., Schelin J., Miskiewicz E., Clarke A.K.;
RT "Novel form of ClpB/HSP100 protein in the cyanobacterium Synechococcus.";
RL J. Bacteriol. 183:7392-7396(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- MISCELLANEOUS: Not induced by heat shock or other stresses, it is
CC expressed constitutively in the cell.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; U97124; AAB72154.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB56669.1; -; Genomic_DNA.
DR RefSeq; WP_011243200.1; NC_007604.1.
DR AlphaFoldDB; O34209; -.
DR SMR; O34209; -.
DR STRING; 1140.Synpcc7942_0637; -.
DR PRIDE; O34209; -.
DR EnsemblBacteria; ABB56669; ABB56669; Synpcc7942_0637.
DR KEGG; syf:Synpcc7942_0637; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_3; -.
DR OMA; GPEHILM; -.
DR OrthoDB; 1115436at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0637-MON; -.
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..895
FT /note="Chaperone protein ClpB 2"
FT /id="PRO_0000191189"
FT DOMAIN 6..148
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 9..74
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 85..148
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 163..346
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 347..557
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 567..778
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 779..895
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 397..533
FT /evidence="ECO:0000250"
FT BINDING 210..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 617..624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 895 AA; 99821 MW; EF5B0103EB513302 CRC64;
MQPTDPNRFT DQAWDAIVES QTVARQLRQQ QLEVEHVLLA LLDQESGVAA EILAKAGVAV
ANLRQPLEDF ARRQPRNASG TQLYLGRGLD RLLDLAERAR ELWQDEFIGV EHLLMGFVED
DRIGRRLAQG LKLDAKTLET TIQALRSPAA DEAEAEESEP SYPFLSKYGR DLTALAEQEK
LDPVIGRDLE IRRVIQVLSR RSKNNPVLIG EPGVGKTAIA EGLAQRIVAG EVPDSLKQRR
LISLDMGSLI AGAKYRGEFE ERLRAVLHEV THSDGQMVLF IDELHTVVGA GAGQQGSAMD
AGNLLKPMLA RGELRCIGAT TTDEYRRTIE KDPALERRFQ QVYVSQPSVE DTIAILRGLK
ERYEGHHGVK ITDGALMAAA KLSHRYISDR FLPDKAIDLI DEASAQLKME ITSKPSELED
LERRLLQLEM EQLSLSGENG QASVHSDRLQ QIQTELQTLQ EQQARLNQQW QQEKQLLEEL
GRLQEEEETL RQQVNQAERE HDLNKGAELK FGQLEALQQQ RQAIEEQIQA LHANGQTLLR
EQVEEADIAE IVARWTNIPV QRLLESERQK LLQLESFLHQ RVIGQDEAVV AVAAAIRRAR
AGMKDPSRPI GSFLFLGPTG VGKTELARAL ANCLFDAEDA LIRFDMSEYM EKNSISRLIG
APPGYIGYEE GGQLSEAIRR HPYAVVLFDE VEKAHPDVFN LLLQVLDDGR ITDSQGRTID
FCNAVIVMTS NIGSQFILEM GEEEASLDAV ELKVLGALRQ HFRPEFLNRI DDTILFQPLS
RGQLQQIVDI QLQRLKRLLA EQAIALNVTP AAAANLADRG YDPVYGARPL KRAIQRLIEN
PVASLILEQQ FDAGDALIVD VDAEGQLQFQ VSKPVTATVV EPDDSPAIAV EAIPS
