GenomeNet

Database: UniProt
Entry: A0A2R5HF02_9LACT
LinkDB: A0A2R5HF02_9LACT
Original site: A0A2R5HF02_9LACT 
ID   A0A2R5HF02_9LACT        Unreviewed;       866 AA.
AC   A0A2R5HF02;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB_2 {ECO:0000313|EMBL:GBG96644.1};
GN   Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=NtB2_00768 {ECO:0000313|EMBL:GBG96644.1};
OS   Lactococcus termiticola.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=2169526 {ECO:0000313|EMBL:GBG96644.1, ECO:0000313|Proteomes:UP000245021};
RN   [1] {ECO:0000313|EMBL:GBG96644.1, ECO:0000313|Proteomes:UP000245021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NtB2 {ECO:0000313|EMBL:GBG96644.1,
RC   ECO:0000313|Proteomes:UP000245021};
RA   Noda S., Aihara C., Yuki M., Ohkuma M.;
RT   "Draft Genome Sequence of Lactococcus sp. Strain NtB2 (JCM 32569), Isolated
RT   from the Gut of the Higher Termite Nasutitermes takasagoensis.";
RL   Genome Announc. 6:e00445-18(2018).
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:GBG96644.1}.
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; BFFO01000004; GBG96644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R5HF02; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000245021; 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:UP000245021};
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          407..501
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   866 AA;  96877 MW;  0A0E70E3E91DE98E CRC64;
     MDIEKMTTSL QQSLAAAQQI AQTRQHQNIE IPHLWRALIE PNSFSENFYK DLGLDTEAFI
     QAIEKEIDKI PTVQGDTIRY GQSLSNELFQ LFNEADKEAK KLGDEYLSTE VLLLALFSLK
     KNALTAYLTA AGIDQKKARE ALEKLRGGER VTSQNAEETY KALEKYGVDL VAQVKSGKQD
     PVIGRDEEIR DVIRVLSRKT KNNPVLIGEP GVGKTAIVEG LAQRIVRRDV PENLKDKTIF
     SLDMGALIAG AKFRGEFEER LKAVLNEVKK SDGQIILFID ELHTIVGAGK TEGSMDAGNL
     LKPMLARGEL HLIGATTLDE YRKYMETDKA LERRFQKVLV TEPTVEDTIS ILRGLKERFE
     IHHSVTIHDN ALVAAATLSN RYITDRFLPD KAIDLVDEAC ATIRVEMNSL PTELDQANRR
     LMQLEIEEAA LKKETDDASK KRLEILRAEI AELREENNQL KAQWEAEKKE VNAISDKRTE
     LEQARHELEE AQNNNDLEAA AALRYGKIPE LEAGLKALEE KSKSEDLSLV QESVTEEQIA
     EVVGRMTGIP ITKLVEGERE KLLHLDETLH QRVVGQDEAV EAVSDAIIRA RAGIQDPNRP
     LGSFLFLGPT GVGKTELAKA LAENLFDSEE HMVRIDMSEY MEKHSVSRLV GAPPGYVGYD
     EGGQLTEAVR RNPYTIILLD EIEKAHPDVF NILLQVLDDG RLTDSKGVLV DFKNTVLIMT
     SNVGSQLLLD GLSDNGELTE ETREAVLSQL RMHFKPEFLN RIDDTILFKP LTIDNVKNII
     VKMTGQLKAR LEEMEVSLEL SDEVQGWIAE NAYEPAYGAR PLKRYLTKAI ENPLAKLIIA
     GKIPAGSKVV VKLVDDKIDF EILASE
//
DBGET integrated database retrieval system