ID A0A1H9IFX7_9LACT Unreviewed; 865 AA.
AC A0A1H9IFX7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05421767_10570 {ECO:0000313|EMBL:SEQ73305.1};
OS Granulicatella balaenopterae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Granulicatella.
OX NCBI_TaxID=137733 {ECO:0000313|EMBL:SEQ73305.1, ECO:0000313|Proteomes:UP000198556};
RN [1] {ECO:0000313|EMBL:SEQ73305.1, ECO:0000313|Proteomes:UP000198556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15827 {ECO:0000313|EMBL:SEQ73305.1,
RC ECO:0000313|Proteomes:UP000198556};
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; FOGF01000005; SEQ73305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9IFX7; -.
DR STRING; 137733.SAMN05421767_10570; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198556; 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:SEQ73305.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEQ73305.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198556};
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..535
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 97684 MW; 599A25378BE1F897 CRC64;
MNIEKMTTTM QQALADAQQI AVVRKHQQID IPHLWKVFLQ PDHFARHLYE GVNAPLEPLD
RIVDQELDRI SVVEGGNVQY GQSITSNLYQ VFAEAEKIRS EFQDEYVAVE VVLLALMHLP
HHPIAKLLIE YGITEKVLKE KIEELRGGER VTSQNQEEQY EALKKYARNL NEAVKSGKQD
PVIGRDEEIR DVIRILSRKT KNNPVLIGEP GVGKTAIIEG LAQRIVRKDV PENLKSKTIF
SLDMGALIAG AKYRGEFEER LKGVLKEVTK ADGEIILFID EIHTIVGAGK TEGSMDAGNL
LKPMLARGEL HCIGATTLDE YRENMEKDKA LERRFQKVLV QEPSVEDTIS ILRGLKERFE
IHHSVNIHDA ALVAAATLSN RYITDRFLPD KAIDLVDEAC ATIRVEMNSM PTELDAVTRR
LMQLEIEEAA LKMEHDDASK KRLATLQEEL AELREEANSL KMKWEIEKEE ANSIRNKREE
IDKARHELEE AESDYNLGRA AELRHGLIPS LERELRELEE KVAEKAGTAE RLVQESVTEE
EIARVVGRLT GIPVTRLVEG EREKLLHLED TLHQRVIGQE EAVAKVSDAV LRSRAGLQNP
NRPIGSFLFL GPTGVGKTEL AKSLAEDLFD SESHMVRIDM SEYMEKFAVS RLVGAPPGYV
GYEEGGQLTE AVRRSPYTIV LLDEIEKAHP DVFNILLQVL DDGRLTDSKG RVVDFTNTVL
IMTSNIGSQY LLDNEGDTIN PETKALVESV LKQQFKPEFL NRIDETIFFT PLSRENIKGI
ITKMTRQLTE RLAEQEITLT LSDEVKEWIG DNAYNPIYGA RPIARYIQRE VETPLAKVMI
KGDVMPGDTI EAQLVDEQVI FAKKS
//