ID A0A1S6QL79_9LACO Unreviewed; 864 AA.
AC A0A1S6QL79;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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=PL11_009340 {ECO:0000313|EMBL:AQW22374.1};
OS Lentilactobacillus curieae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1138822 {ECO:0000313|EMBL:AQW22374.1, ECO:0000313|Proteomes:UP000030361};
RN [1] {ECO:0000313|EMBL:AQW22374.1, ECO:0000313|Proteomes:UP000030361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC M 2011381 {ECO:0000313|EMBL:AQW22374.1,
RC ECO:0000313|Proteomes:UP000030361};
RX PubMed=26021929;
RA Wang Y., Wang Y., Lang C., Wei D., Xu P., Xie J.;
RT "Genome Sequence of Lactobacillus curieae CCTCC M 2011381T, a Novel
RT Producer of Gamma-aminobutyric Acid.";
RL Genome Announc. 3:0-0(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}.
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DR EMBL; CP018906; AQW22374.1; -; Genomic_DNA.
DR RefSeq; WP_035167670.1; NZ_CP018906.1.
DR AlphaFoldDB; A0A1S6QL79; -.
DR KEGG; lcu:PL11_009340; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000030361; Chromosome.
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:UP000030361};
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 49..76
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 414..501
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 95800 MW; D765CE50AC24F315 CRC64;
MNPDNLTEAV STAISSAQQI AVTRKQQNIT VAHLFKALVQ PGELARQIYS ELGLDLNALE
RELDKEIDAI AVVEGSSITY GQSLSANLYE LLQNAEQVKN KFDDKFIAVD TLTIALMRLH
GDKFKDYLAS QDVTEQKVQN VVENIRGGQK VVNKNQEDSY QSLEKYGTDL VKAARENKLG
PIIGRDQEIL EVVTILSRKN KNNPVLIGAP GVGKTAVVEG LAKRIASNDV PENLKDKTIY
QLDMGSLIAG AKYRGEFEER LQAVLKEVRK SEGQIIMFID EIHNIVGAGK AEGSMDAGNI
LKPMLARGEL HLIGATTIDE YRKYMEKDKA LERRFQRVLV EEPTVEDTIT ILRGLRESLE
IHHGVRIHDN ALVAAAKLSD RYITDRNLPD KAIDLVDEAS AEIRVVMNSQ PTELDSANRQ
LMRLEVEEAA LKQETDAASK KRLASVQKEL ASIQERVNEL NARWGSEKQS IQHISDVKRK
LDQAKNDLVN AENNYDLDKA AVLQHGTIPD LEKEINDLES NDQHDDWLVS ESVTSEEIAN
VVSRQTGIPV NKLVEGERQK LLKLADNLHR RVIGQDAAVT AVSDAVLRSR AGLADPSKPL
GSFLFLGPTG VGKTELAKAL AEDLFDSENH MVRIDMSEYM EKESVSRLVG AAPGYVGYEE
GGQLTEAVRR NPYTIVLFDE IEKAHPDVFN ILLQVLDDGR LTDSQGRTIN FKNTILIMTS
NLGSDILLSG TDENGKISDQ AKQQVEKLLQ VSFKPEFLNR IDDVITFAPL TKENIKQIVQ
KIIDHLSART KAQSITLKIT DAAKQWVADN GYDPQYGARP LQRFVTNQVE TPIAKMIIGD
EIAAGSTVLI DIVADQLAFS TTNK
//