GenomeNet

Database: UniProt
Entry: A0A4S3B934_9ENTE
LinkDB: A0A4S3B934_9ENTE
Original site: A0A4S3B934_9ENTE 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system