ID A0A1H9R8G1_9LACT Unreviewed; 871 AA.
AC A0A1H9R8G1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04488559_10386 {ECO:0000313|EMBL:SER68243.1};
OS Isobaculum melis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Isobaculum.
OX NCBI_TaxID=142588 {ECO:0000313|EMBL:SER68243.1, ECO:0000313|Proteomes:UP000198948};
RN [1] {ECO:0000313|EMBL:SER68243.1, ECO:0000313|Proteomes:UP000198948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13760 {ECO:0000313|EMBL:SER68243.1,
RC ECO:0000313|Proteomes:UP000198948};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FOHA01000003; SER68243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9R8G1; -.
DR STRING; 142588.SAMN04488559_10386; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198948; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Hydrolase {ECO:0000313|EMBL:SER68243.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SER68243.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198948};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 98308 MW; 389A97D02406EB5A CRC64;
MELEKMTTTM QQALGDAQQI AVTRHHQTID IAHLWKIFMT PDHFTRNLYQ DVGLDIAGFE
QLIDQELEQY PVIEGSSVAY GQNLSQNLFQ LLTEADKIRG QFEDEYLATE IVVLALMKLK
NHPLTKYLVS QGVTEKELKK AIEEIRGGEK VTSLNQEEQY KALEKYGTDL VQAVKSGKQD
PVIGRDEEIR DVIRILSRKT KNNPVLIGEP GVGKTAIVEG LAQRIVRKDV PENLKDKTIF
SLDMGALIAG AKFRGEFEER LKAVLKEVKK SDGRIILFID EIHTIVGAGK TEGSMDAGNL
LKPMLARGEL HCIGATTLDE YRQYMETDKA LERRFQKVLV NEPTVEDTIS ILRGLKERFE
IHHSVNIHDN ALVAAATLSN RYITDRFLPD KAIDLVDEAC ATIRVEMNSM PNELDQVTRR
LMQLEIEEAA LKKEKDDASK KRLETIQQEL ADLRESANNM KMKWETEKEE VSKVRDKRAI
LEQLRRELED AESNYNLERA AELRHGTIPQ VEKELHVLEQ ENEEKQKGSS RLVQESVTEN
EIAEVIARMT GIPVTRLVEG EREKLLKLGE TLHKRVIGQD EAVQMVTDAV IRARAGLQDP
TRPLGSFLFL GPTGVGKTEL AKALAENLFD SEEHMVRIDM SEYMEKHSVS RLVGAPPGYV
GYEEGGQLTE AVRRSPYTIV LLDEIEKAHP DVFNILLQVL DDGRLTDSKG RVVDFKNTVL
IMTSNIGSHL LLEGLDVLTG ELKPEVEDGV YNLLKSSFKP EFLNRIDDTV LFKPLTLDNV
KGIVEKMTVS LTQRLAEQEI TLSLSDEALA FVAENAYDPV YGARPLKRYL TKEVETPLAR
EIIAGKILPK TKVLVTVKED QLAFEYLNET L
//