ID A0A4S3B934_9ENTE Unreviewed; 867 AA.
AC A0A4S3B934;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:THB61505.1};
GN ORFNames=ESZ54_04615 {ECO:0000313|EMBL:THB61505.1};
OS Vagococcus silagei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=2508885 {ECO:0000313|EMBL:THB61505.1, ECO:0000313|Proteomes:UP000310506};
RN [1] {ECO:0000313|EMBL:THB61505.1, ECO:0000313|Proteomes:UP000310506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2B-2 {ECO:0000313|EMBL:THB61505.1,
RC ECO:0000313|Proteomes:UP000310506};
RA Guu J.-R.;
RT "Vagococcus silagei sp. nov. isolated from brewer's grain.";
RL Submitted (JAN-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:THB61505.1}.
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DR EMBL; SDGV01000011; THB61505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S3B934; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000310506; 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:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000310506};
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 867 AA; 97883 MW; EA9B5C7CBD75DC57 CRC64;
MNIEKMTTTL QQSITEAQQI AMTRKQQEID IAHLWKIFVQ PNHFARNLYQ DAGLDVNQFE
AEIDRQIDKL PQVAGSNVQY GQSMSQNLFN LFNEADQIRT QFNDDFVATE VVVLALFKLK
NHALTVYLND YGITEKALKE KIESIRGGDR VTSQNQEEQY EALEKYGIDL VKAVKEGKQD
PIIGRDEEIR DVIRILSRKT KNNPVLIGEP GVGKTAIIEG LAQRIVRKDV PENLKDKTIF
SLDMGALIAG AKYRGEFEER LKAVLKEIKK SDGQIILFID EIHTIVGAGK TEGSMDAGNL
LKPMLARGEL HCIGATTLDE YRENMEKDKA LERRFQKVLV KEPTVEDTIS ILRGLKERFE
IHHGVDIHDN ALVSAATLSN RYITDRFLPD KAIDLVDEAC ATIRVEMNSM PTELDQVTRR
LMQLEIEEAA LKKEDDDASM KRLEILQKEL SGLREETNTL KMQWETEKEE VNKISDKRAE
IDQAKTQLEN AEINYDLEEA AVLRHGTIPK LQKELAELEQ TTKGETARLV QEVVTEKEIA
TVVGRLTGIP VSKLEEGERE KILRLNETLH QRVIGQEEAV NAVADAVIRS RAGLQDPDRP
LGSFLFLGPT GVGKTELAKA LAENLFDSEE HMVRIDMSEY MEKHSVSRLV GAPPGYIGYE
EGGQLTEAVR RSPYTIVLLD EIEKAHPDVF NILLQVLDDG RLTDSKGRVV DFKNTVLIMT
SNLGSQMLLE GTDAEGTINE EAKNSVMSLL KAHFKPEFLN RIDDTILFTP LSLENVKGII
VKMMEALSRR LQDQDIFIEL SEAAKDWIAE QAYDPIYGAR PIKRFLTREI ETPLAKEIIG
GKILPKTQIL VEEVDGHLEF LKTPIEE
//