ID A0A0R1KRP1_9LACO Unreviewed; 868 AA.
AC A0A0R1KRP1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=FC99_GL002289 {ECO:0000313|EMBL:KRK85800.1};
OS Levilactobacillus koreensis JCM 16448.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423819 {ECO:0000313|EMBL:KRK85800.1, ECO:0000313|Proteomes:UP000050910};
RN [1] {ECO:0000313|EMBL:KRK85800.1, ECO:0000313|Proteomes:UP000050910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16448 {ECO:0000313|EMBL:KRK85800.1,
RC ECO:0000313|Proteomes:UP000050910};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRK85800.1}.
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DR EMBL; AZDP01000123; KRK85800.1; -; Genomic_DNA.
DR RefSeq; WP_048735984.1; NZ_AZDP01000123.1.
DR AlphaFoldDB; A0A0R1KRP1; -.
DR STRING; 637971.ABN16_12285; -.
DR PATRIC; fig|1423819.3.peg.2454; -.
DR Proteomes; UP000050910; 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 78, MITOCHONDRIAL; 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 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..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 96475 MW; 5B94D19B18117C01 CRC64;
MNPEKMTQAL TDALTEAQHI AMTRKHQAVT VAHLFKFLIQ PGELGREILA DAGANIADLD
SELDRELDAI STVSGSGIQY GQEFSRNLTE LLQKADAVKD GYHDEFMAVD TVLIAVMQLN
GENLTDYLKS QGMTEQLVRN AVDKVRGGER VTSKNQEDQY KALEKYGIDL VKAMRSGKID
PIIGRDDEIL SVIRILSRKT KNNPVLIGEA GVGKTAIVEG LAQRIVRGDV PDNLKDKTIF
SLDMGSLIAG AKYRGEFEER LKAVLKEVTK SDGQIIMFID EIHNIVGAGK AEGSMDAGNL
LKPMLARGEL HLIGATTLDE YREYLEKDKA LARRFQRVLV NEPSIDDTVT ILRGLRERFE
IHHGVKIHDN ALIAAAKLSD RYLTDRFLPD KAIDLVDEAS ASIRVEMNSA PTELDQARRQ
MMRMQVEQTA LKQETDEASQ KRLTELNKEL ADIKEKVDKL SAQWNQEKTA IKSVGDKKTE
LDTAKRDLEN AESAYDLNKA AELQHGTIPR LQKELAELEK QDQNQNWLVS ESVTENEIAA
VVSRMTGIPV TKLVQGEREK LLKLADRLHD RVVGQDQAVS AVADAVLRSR AGLQDPTKPL
GSFLFLGPTG VGKTELAKAL AENLFDSEDH MVRIDMSEYM EKESVSRLVG AAPGYVGYEE
GGQLTEAVRR NPYTIVLFDE VEKAHPDVFN LLLQVLDDGR LTDSQGRTVD FKNTILIMTS
NLGSELLLRG TDDQGRISPD AQKQVAQLLQ THFRPEFLNR IDETIMFTPL SLADVQQIVV
KLVAHLAVRL HEQQLDLTIT PVAQAWIAKS GYLPAYGARP LQRFITTHVE TPLAKQLIAG
KIPVNSLITI DVADDQLQFT HTPMAVKE
//
