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Database: UniProt
Entry: A0A0R1S6M1_9LACO
LinkDB: A0A0R1S6M1_9LACO
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ID   A0A0R1S6M1_9LACO        Unreviewed;       868 AA.
AC   A0A0R1S6M1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=FC85_GL001264 {ECO:0000313|EMBL:KRL64249.1};
OS   Lentilactobacillus diolivorans DSM 14421.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=1423739 {ECO:0000313|EMBL:KRL64249.1, ECO:0000313|Proteomes:UP000052013};
RN   [1] {ECO:0000313|EMBL:KRL64249.1, ECO:0000313|Proteomes:UP000052013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14421 {ECO:0000313|EMBL:KRL64249.1,
RC   ECO:0000313|Proteomes:UP000052013};
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:KRL64249.1}.
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DR   EMBL; AZEY01000093; KRL64249.1; -; Genomic_DNA.
DR   RefSeq; WP_057865705.1; NZ_AZEY01000093.1.
DR   AlphaFoldDB; A0A0R1S6M1; -.
DR   STRING; 1423739.FC85_GL001264; -.
DR   PATRIC; fig|1423739.3.peg.1320; -.
DR   Proteomes; UP000052013; 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:UP000052013};
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..101
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          414..501
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   868 AA;  96745 MW;  C8FA13F747D654E1 CRC64;
     MNPDNLTEAV TQAISQAQQI ATTRKQQNIT VAHLFKFLVQ PGELARQIYS DLGLNLDDLN
     SELDNEIDQI ATVEGSNVNY GQSLSANLYE LLQNAEQLKN EFGDSFIAVD TLTIAVMGLH
     GDKFTDYLKQ HDITEQKVRN VVEKIRGGQK VTSKNQEDSY QALEKYGTDL VKAARANKLG
     PIIGRDEEIL DVIRVLSRKT KNNPVLIGAP GVGKTAVVEG LAIRIANNDV PENLKNKTIF
     QLDMGSLIAG AKYRGEFEER LQSVLKEVKK AEGQIIMFID EIHNIVGAGK AEGSMDAGNI
     LKPMLARGEL HLIGATTLDE YRKYMEKDKA LERRFQRVVV HEPTVEDTIT ILRGLAESLE
     IHHGVRIHDN ALVAAAKLSD RYITDRYLPD KAIDLVDEAS AEIRVEMNSS PTELDQSNRQ
     LMRLEVEEAS LKQETDEASK NRLKQLQSEL ANTKERVNTL NARWKQEKDS IKKISDKKKQ
     LDQAKNDLKQ AENNYDLNKA AVLQHGTIPE LETDLKKLET NDQHADWLVS ESVTANEIAS
     VVSRETGIPV TKLVEGERKK LLHLADNLHK RVIGQDAAVT AVSDAVIRSR AGLQDPSRPL
     GSFLFLGPTG VGKTELAKAL AEDLFDSEDH MVRIDMSEYM EKESVSRLVG AAPGYVGYEE
     GGQLTEAVRR NPYTIVLFDE IEKAHPDVFN ILLQVLDDGR LTDSQGRTIN FKNTILIMTS
     NLGSDILLEG TDENGVISTD AKKQVNQLLR ASFKPEFLNR IDDVITFTPL SRSDIEKIVQ
     KLIDQLSNRT KAQDVTISIS DDAKSWIAKN GYEPQYGARP LQRYVTNVVE TPLAKMMIAD
     QIKSHSIVHI NLDNDQLTFV PELVPQNG
//
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