CLPB1_SYNE7
ID CLPB1_SYNE7 Reviewed; 874 AA.
AC P53533; Q31PA0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Chaperone protein ClpB 1;
GN Name=clpB1; OrderedLocusNames=Synpcc7942_1089;
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=8759846; DOI=10.1128/jb.178.16.4839-4846.1996;
RA Eriksson M.J., Clarke A.K.;
RT "The heat shock protein ClpB mediates the development of thermotolerance in
RT the cyanobacterium Synechococcus sp. strain PCC 7942.";
RL J. Bacteriol. 178:4839-4846(1996).
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.
RN [3]
RP ALTERNATIVE INITIATION, AND ROLE IN THERMOTOLERANCE.
RX PubMed=9260953; DOI=10.1128/jb.179.16.5111-5117.1997;
RA Porankiewicz J., Clarke A.K.;
RT "Induction of the heat shock protein ClpB affects cold acclimation in the
RT cyanobacterium Synechococcus sp. strain PCC 7942.";
RL J. Bacteriol. 179:5111-5117(1997).
RN [4]
RP ROLE OF ISOFORM CLP' IN THERMOTOLERANCE.
RX PubMed=11092876; DOI=10.1128/jb.182.24.7092-7096.2000;
RA Clarke A.K., Eriksson M.J.;
RT "The truncated form of the bacterial heat shock protein ClpB/HSP100
RT contributes to development of thermotolerance in the cyanobacterium
RT Synechococcus sp. strain PCC 7942.";
RL J. Bacteriol. 182:7092-7096(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 Necessary for thermotolerance. {ECO:0000250,
CC ECO:0000269|PubMed:9260953}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=ClpB;
CC IsoId=P53533-1; Sequence=Displayed;
CC Name=ClpB';
CC IsoId=P53533-2; Sequence=VSP_018706, VSP_018707;
CC -!- INDUCTION: By heat shock.
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: [Isoform ClpB']: Also contributes to the overall
CC thermotolerance of the bacterium. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB09631.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABB57119.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U20646; AAB09631.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000100; ABB57119.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_039755993.1; NC_007604.1.
DR AlphaFoldDB; P53533; -.
DR SMR; P53533; -.
DR STRING; 1140.Synpcc7942_1089; -.
DR PRIDE; P53533; -.
DR EnsemblBacteria; ABB57119; ABB57119; Synpcc7942_1089.
DR KEGG; syf:Synpcc7942_1089; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_3; -.
DR OrthoDB; 44062at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1089-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 2: Evidence at transcript level;
KW Alternative initiation; ATP-binding; Chaperone; Coiled coil; Cytoplasm;
KW Nucleotide-binding; Repeat; Stress response.
FT CHAIN 1..874
FT /note="Chaperone protein ClpB 1"
FT /id="PRO_0000005497"
FT DOMAIN 6..148
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 85..148
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 161..342
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 343..551
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 561..772
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 773..874
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 393..527
FT /evidence="ECO:0000250"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 611..618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..150
FT /note="Missing (in isoform ClpB')"
FT /evidence="ECO:0000305"
FT /id="VSP_018706"
FT VAR_SEQ 151
FT /note="V -> M (in isoform ClpB')"
FT /evidence="ECO:0000305"
FT /id="VSP_018707"
FT CONFLICT 262
FT /note="K -> T (in Ref. 1; AAB09631)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="I -> M (in Ref. 1; AAB09631)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="P -> T (in Ref. 1; AAB09631)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..320
FT /note="DE -> GK (in Ref. 1; AAB09631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 874 AA; 98726 MW; 4F77180DA08FD140 CRC64;
MQPTNPNQFT EKAWEAIVRT TDVAKQAQHQ QIESEHLFLA LLQEPGLALN ILKKAGLEAA
QLQQFTERFI ARQPKVSGGN QSVYLGRSLD QLLDQADQFR KDFGDEFISV EHLILSFPRD
SRFGRLLSQE FKVDEKQLRQ IIQQIRGSQK VTDQNPEGKY EALEKYGRDL TEMARRGKLD
PVIGRDDEIR RTIQILSRRT KNNPVLIGEP GVGKTAIAEG LAQRIINGDV PQSLKDRRLI
ALDMGALIAG AKFRGEFEER LKAVLKEVTD SEGIIILFID EIHTVVGAGA VQGSMDAGNL
LKPMLARGEL RCIGATTLDE YRQYIEKDAA LERRFQQVFV DQPTVEDTIS ILRGLKERYE
VHHGVRISDN ALVAAAVLST RYISDRFLPD KAIDLVDESA ARLKMEITSK PEELDEIDRK
ILQLEMERLS LQKESDLASQ ERLQRLEKEL ADLKEEQRSL SSQWQAEKDV ITDIQSVKEE
IDQVNLLIQQ AERDYDLNKA AELKYGKLTE LQRKLNEMEG GLATTHTSGK SLLREEVTEV
DIAEIISKWT GIPVSKLVES EMQKLLNLDE ELHQRVIGQE EAVSAVADAI QRSRAGLSDP
KRPIASFIFL GPTGVGKTEL AKALAAYLFD TEDAMIRIDM SEYMEKHAVS RLIGAPPGYV
GYDEGGQLTE AVRRRPYSVI LFDEIEKAHP DVFNVMLQIL DDGRVTDSRG RTVDFKNTIL
ILTSNIGSQY ILDVAGDDSR YEEMRSRVTE ALRANFRPEF LNRVDETIIF HSLRKDQLQQ
IVRIQLHRLE ERLSDRKLSL SMSPEAIDFL VEIGFDPVYG ARPLKRVIQR ELETAIAKAI
LRGQFSDGDT IQVAVENERL VFKAIATPTA VPLS
