CLPB_LACLM
ID CLPB_LACLM Reviewed; 867 AA.
AC O68185; A2RJX3; Q9S5Z3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=llmg_0986;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Coward C.;
RT "Chaperones and ATP-dependent proteases of Lactococcus lactis.";
RL Thesis (1998), University of Cambridge, United Kingdom.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-392, ALTERNATIVE INITIATION, AND
RP INDUCTION.
RX PubMed=10094684; DOI=10.1128/jb.181.7.2075-2083.1999;
RA Ingmer H., Vogensen F.K., Hammer K., Kilstrup M.;
RT "Disruption and analysis of the clpB, clpC, and clpE genes in Lactococcus
RT lactis: clpE, a new Clp family in Gram-positive bacteria.";
RL J. Bacteriol. 181:2075-2083(1999).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=ClpB;
CC IsoId=O68185-1; Sequence=Displayed;
CC Name=ClpB';
CC IsoId=O68185-2; Sequence=VSP_018704, VSP_018705;
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:10094684}.
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; AF016634; AAC16900.1; -; Genomic_DNA.
DR EMBL; AM406671; CAL97579.1; -; Genomic_DNA.
DR EMBL; AF023423; AAD01784.1; -; Genomic_DNA.
DR RefSeq; WP_011834922.1; NZ_WJVF01000049.1.
DR AlphaFoldDB; O68185; -.
DR SMR; O68185; -.
DR STRING; 416870.llmg_0986; -.
DR EnsemblBacteria; CAL97579; CAL97579; llmg_0986.
DR KEGG; llm:llmg_0986; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_9; -.
DR OMA; GPEHILM; -.
DR PhylomeDB; O68185; -.
DR BioCyc; LLAC416870:LLMG_RS05015-MON; -.
DR Proteomes; UP000000364; 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 2: Evidence at transcript level;
KW Alternative initiation; ATP-binding; Chaperone; Coiled coil; Cytoplasm;
KW Nucleotide-binding; Repeat; Stress response.
FT CHAIN 1..867
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000005493"
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..70
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 84..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..548
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 558..770
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 771..867
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 608..615
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_018704"
FT VAR_SEQ 151
FT /note="V -> M (in isoform ClpB')"
FT /evidence="ECO:0000305"
FT /id="VSP_018705"
FT CONFLICT 358
FT /note="R -> C (in Ref. 3; AAD01784)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="V -> I (in Ref. 1; AAC16900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 867 AA; 97327 MW; C2A3E907F0BAC573 CRC64;
MDIEKMTTTM QEALGSAQQI AQVRHHQVIE VPHLWRIFVQ PNSFGANFYK DLGIDLDDFT
NLIEKEIDKI NSVEGSNITY GQNLSPDLFQ VFTEADKIAQ KMGDEYLSTE IILLALFELK
QNPLTEYLVS HGLTKAKAQA AIEKLRGGDK VTSQNAEETY KALEKYGVDL VAQVKSGNQD
PVIGRDEEIR DVIRVLSRKT KNNPVLIGEP GVGKTAIVEG LAQRIVRKDV PENLKDKTIF
SLDMGALIAG AKYRGEFEER LKAVLNEVKK ADGQIILFID ELHTIVGAGK TEGSMDAGNL
LKPMLARGEL HLIGATTLDE YRKYMETDKA LERRFQKVLV TEPTVEDTIS ILRGLKERFE
IHHGVTIHDN ALVAAATLSN RYITDRFLPD KAIDLIDEAS ATIRVEMNSL PTELDQANRR
LMQLEIEEAA LKKERDDASK KRLEIIRGEI AELREENNQL KAQWEAEKKE VGNISEKRNE
LEHARHELEE AQNEGNLEKA AALRYGKIPE IEKELKAIEE KAKSDDLSLV QESVTEEQIA
EVVGRMTGIP ITKLVEGERE KLLHLPETLH QRVVGQDEAV EAVSDAIIRA RAGIQDPNRP
LGSFLFLGPT GVGKTELAKA LAENLFDSEE HMVRIDMSEY MEKHSVSRLV GAPPGYVGYD
EGGQLTEAVR RNPYTIILLD EIEKAHPDVF NILLQVLDDG RLTDSKGVLV DFKNTVLIMT
SNVGSQYLLD NVGENGEISE ETTENVMSQL RAHFKPEFLN RIDDTILFKP LALEDIKNII
LKMTSQLAHR LEEMEVELEL SEEVKVWIAE NAYEPAYGAR PLKRYLTKVI ENPLAKLIIG
GKIPPKSKVI VRLIDNKVDF DVQSIAE
