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Database: UniProt
Entry: A0A1H9R8G1_9LACT
LinkDB: A0A1H9R8G1_9LACT
Original site: A0A1H9R8G1_9LACT 
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
//
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