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Database: UniProt
Entry: G8TFE0_NIAKG
LinkDB: G8TFE0_NIAKG
Original site: G8TFE0_NIAKG 
ID   G8TFE0_NIAKG            Unreviewed;       870 AA.
AC   G8TFE0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Niako_0971 {ECO:0000313|EMBL:AEV97350.1};
OS   Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS   GR20-10).
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niastella.
OX   NCBI_TaxID=700598 {ECO:0000313|EMBL:AEV97350.1, ECO:0000313|Proteomes:UP000005438};
RN   [1] {ECO:0000313|EMBL:AEV97350.1, ECO:0000313|Proteomes:UP000005438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC   {ECO:0000313|Proteomes:UP000005438};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA   Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Niastella koreensis GR20-10.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU362034}.
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; CP003178; AEV97350.1; -; Genomic_DNA.
DR   RefSeq; WP_014217264.1; NC_016609.1.
DR   AlphaFoldDB; G8TFE0; -.
DR   STRING; 700598.Niako_0971; -.
DR   KEGG; nko:Niako_0971; -.
DR   PATRIC; fig|700598.3.peg.994; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_10; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000005438; 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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          404..529
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   870 AA;  97781 MW;  3BDEF9F7CE6B3B19 CRC64;
     MNLGNFTIKA AEAFQQAQQL AFNSQSPNIE TEHVLKALLD QEDSPVEYLL KKNNVTVNLL
     ENKLQESINK LPKTSGDAAQ SVSREANNVV LRAGAVLKQF GDEFITPEHL LLAIVQGNDS
     TARLLKEAGL SEKGLVTAIK ELRKGETVQS QTQETTFNAL NKYARNLNDL ARQGKLDPVI
     GRDEEIRRTL HILSRRTKNN PILVGEPGVG KTAIAEGIAH RIVNGDVPEN LKTKVIYTLD
     MGQLIAGAKY KGEFEERLKG VVKDVTESNG EIILFIDEIH TLVGAGGGEG AMDAANILKP
     ALARGELRAI GATTLNEYQR YFEKDKALER RFQKVMIDEP SVEDAISILR GLKDRYETHH
     HVRIKDEAII AAVELSSRYI TDRFLPDKAI DLIDEAAAKL RLEMNSMPEE LDHLIRQIRQ
     LEIEREAIKR ENDEEKLKEL NTEIANLSVQ RDTLKAKWQE EKELVDKVQD AKAQVEQLKV
     QAEQAERNGD YGTVAEIRYG KIKEQERLIG EYSQQLNAIS ENKRLMKEEV DAEDIAETIA
     KSTGIPVSRM LQSDKEKLLY LEEKLHERVV GQDEAITAVA DAIRRSRAGL HDPKKPIGSF
     IFLGTTGVGK TELAKALADY LFDDESMMTR IDMSEYQEKH TVSRLVGAPP GYVGYEEGGQ
     LTEAVRRKPY SVVLLDEIEK AHPDVWNVLL QVLDDGRLTD AKGRVVNFKN TIIIMTSNIG
     SHLIQEAFEN VKENDVEAAT ERAKVEVMNL LRQTIRPEFL NRVDEVIMFQ PLLKQQIMGI
     VQIQLNSLKR QVAENGIDLR FSNYALEYLA EQGFDIQFGA RPLKRLIQKE IVNPLSKKIL
     AADIDKSKPV MVDVFDGVVV FRNEAPEKVK
//
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