CLPB_LEPBY
ID CLPB_LEPBY Reviewed; 873 AA.
AC O87444;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB;
OS Leptolyngbya boryana (Plectonema boryanum).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Leptolyngbyaceae; Leptolyngbya.
OX NCBI_TaxID=1184;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=UTEX 485 / CCAP 1462/4;
RX PubMed=9748452; DOI=10.1128/jb.180.19.5173-5182.1998;
RA Celerin M., Gilpin A.A., Schisler N.J., Ivanov A.G., Miskiewicz E.,
RA Krol M., Laudenbach D.E.;
RT "ClpB in a cyanobacterium: predicted structure, phylogenetic relationships,
RT and regulation by light and temperature.";
RL J. Bacteriol. 180:5173-5182(1998).
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:0000269|PubMed:9748452}.
CC -!- INDUCTION: By stress conditions, such as excess light and low
CC temperatures. {ECO:0000269|PubMed:9748452}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAC62621.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF061279; AAC62621.1; ALT_INIT; Genomic_DNA.
DR PRIDE; O87444; -.
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 ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding; Repeat;
KW Stress response.
FT CHAIN 1..873
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191155"
FT DOMAIN 6..149
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..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..552
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 562..773
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 774..873
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 394..528
FT /evidence="ECO:0000250"
FT BINDING 209..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 612..619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 873 AA; 99305 MW; CDA07B752CCAE3B2 CRC64;
MQPTNSEKFT EKVWEAIYRT QEMYKQAQQQ QIETEHLMKA LLEQDGLAIS IFNKLAVPVD
RVRDRTDDFI RRQPKVSGSG TSVYWGRRAD ALLXRAEEYR KQFEDSFISI EHLLLGYAQD
SRFGKALLSE FRYPDEAKLR NAIEQVRGNQ KVTDQTPENK YESLEKYGRD LTQYAREGKL
DPVIGRDDEI RRTIQILSRR TKNNPVLIGE PGVGKTAIAE GLAQRILSGD VPQSLKDRKL
IALDMGALIA GAKYRGEFEE RLKAVLKEVT DSRGNIILFI DEIHTVVGAG ATQGAMDAGN
LLKPMLARGE LRCIGATTLD EYRKYIEKDA ALERRFQQVF VDQPSVEDTI SILRGLKERY
EVHHGVKISD SALVAAATLS TRYISDRFLP SKAIDLVDEA AAKLKMEITS KPEELDEVDR
KVLQLEMERL SLQKENDAGS RDRLERLERE LADFKEDQSK LNAQWQAEKS VITDLQKLKE
EIDRVNLEIQ QAERDYDLNR AAELKYGKLN ELNRKVEETE SQLSQIQKSG ATLLREEVLE
SDIAEIISKW TGIPVSKLVE SEMQKLLQLD DVLHQRVIGQ DEAVTAVSDA IQRSRAGLSD
PNRPTASFIF LGPTGVGKTE LAKALAAFLF DTEEAMVRID MSEYMEKHSV SRLIGAPPGY
VGYEEGGQLT EAVRRRPYSV ILFDEIEKAH PDVFNVMLQI LDDGRVTDSQ GRTVDFKNTI
IIMTSNIGSQ YIFEYGGDDD RYEEILSRVM EAMLSNFRPE FLNRIDEIII FHSLQKAQLR
EIVKIQTHRL ESRLARKMSL KLSDAALDFL AEGFDPVYGA RPLKRAIQRE LETTIAKEIL
RSNFTEGDTI FVDVGETERL EFKRLPSEVL TTQ
