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}.
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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
//