GenomeNet

Database: UniProt
Entry: A0A1S6QL79_9LACO
LinkDB: A0A1S6QL79_9LACO
Original site: A0A1S6QL79_9LACO 
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}.
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; 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
//
DBGET integrated database retrieval system