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Database: UniProt
Entry: A0A1E5KY67_9ENTE
LinkDB: A0A1E5KY67_9ENTE
Original site: A0A1E5KY67_9ENTE 
ID   A0A1E5KY67_9ENTE        Unreviewed;       867 AA.
AC   A0A1E5KY67;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BCR26_11740 {ECO:0000313|EMBL:OEH82795.1};
OS   Enterococcus rivorum.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=762845 {ECO:0000313|EMBL:OEH82795.1, ECO:0000313|Proteomes:UP000095256};
RN   [1] {ECO:0000313|EMBL:OEH82795.1, ECO:0000313|Proteomes:UP000095256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25899 {ECO:0000313|EMBL:OEH82795.1,
RC   ECO:0000313|Proteomes:UP000095256};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-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}.
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:OEH82795.1}.
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DR   EMBL; MIEK01000015; OEH82795.1; -; Genomic_DNA.
DR   RefSeq; WP_069698238.1; NZ_MIEK01000015.1.
DR   AlphaFoldDB; A0A1E5KY67; -.
DR   STRING; 762845.BCR26_11740; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000095256; 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:UP000095256};
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;  98053 MW;  0BBFC4E65AC956FC CRC64;
     MNIEKMTTTL QEAIAEAQKI AVTRRHQEID IAHLWKIFLQ PNHFGRNFYT DAGVDVEAFE
     REIDKALDEY PSIQGENIQY GRSMSQNLFN LLNEADKLRE SFHDEFLSTE IVLLGLMKLK
     NYRLTKYLVS QGINEKELRQ NIEAMRGGDR VTSQNQEEQY EALEKYGVDL VQQVKSGNQD
     PIIGRDEEIR DVIRILSRKT KNNPVLIGEP GVGKTAIIEG LAQRIVKRDV PENLKDKTIF
     SLDMGALIAG AKFRGEFEER LKAVLKEVKK SDGRIILFID EIHNIVGAGK TEGSMDAGNL
     LKPMLARGEL HLIGATTLDE YQQYMEKDKA LERRFQRVLV KEPSVEDTIS ILRGLKERFE
     IHHSVNIHDN ALVAAATLSD RYITDRFLPD KAIDLVDEAS ATIRVEMNSM PTELDQVTRR
     LMQLEIEEAA LKKESDDASK KRLGILQEEL AELREETNAM KMQWETEKEE VNAVSNKRAE
     IDKAKHELED AENNYDLERA AVLRHGTIPE LEKELQVLEA KNNSENSKMV QESVTENEIA
     VVVGRLTGIP VTKLVEGERE KLMKLNETLH KRVIGQDEAV DAVSDAVIRS RAGLQDPDRP
     LGSFLFLGPT GVGKTELAKA LAEDLFDSED HMVRIDMSEY MEKHSVSRLV GAPPGYVGYE
     EGGQLTESVR RNPYTIVLLD EIEKAHPDVF NILLQVLDDG RLTDSKGRVV DFKNTVLIMT
     SNIGSQLLLE GVTAEGTIPE EIEEQVMTIL KGNFKPEFLN RIDDTILFTP LSLENVKGII
     EKMTAYLAKR LEQQEIQLVI SDEAKTWIAE SAYEPAYGAR PLKRFITKEV ETPLAKEIVS
     GRIMPKTKVT ISLLNNQLVF ENEAIEE
//
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