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Database: UniProt
Entry: E8WZB7_GRATM
LinkDB: E8WZB7_GRATM
Original site: E8WZB7_GRATM 
ID   E8WZB7_GRATM            Unreviewed;       888 AA.
AC   E8WZB7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=AciX9_0648 {ECO:0000313|EMBL:ADW67719.1};
OS   Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN   [1] {ECO:0000313|Proteomes:UP000000343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA   Haggblom M.M., Woyke T.;
RT   "Complete sequence of chromosome of Acidobacterium sp. MP5ACTX9.";
RL   Submitted (JAN-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; CP002480; ADW67719.1; -; Genomic_DNA.
DR   RefSeq; WP_013579047.1; NC_015064.1.
DR   AlphaFoldDB; E8WZB7; -.
DR   STRING; 1198114.AciX9_0648; -.
DR   PaxDb; 1198114-AciX9_0648; -.
DR   KEGG; acm:AciX9_0648; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_0; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000000343; 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};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000343};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          5..150
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          528..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   888 AA;  97635 MW;  14206C9BC485636A CRC64;
     MAIRWDRLTV KSQEAVQAAS GFAAENGNPE VLPVHLMAAL LEDREGVVIP VLEKIGVPVE
     QMLSGVNAAI AKLPKVQGGT QPGLSNGMQK VIEQAFKEAE NFKDEYCSTE HLLLALSASG
     AGSDTVRSAL AAFGATHEAI LKALSGVRGN TRVTDQTPEG KFQALEKYAK DLTELARRGK
     LDPVIGRDEE IRRVVQVLSR RTKNNPVLIG EPGVGKTAIV EGLARRIVSG DVPESLKDKR
     VVALDLASMV AGAKFRGEFE ERLKAVLKEI EDADGEIILF IDELHTLVGA GAAEGAMDAS
     NMLKPALARG GLRAIGATTL NEYRKYIEKD AALERRFQVV YVGEPNVEDT VAILRGLKER
     YESHHKIRIK DSAIVAAATL SHRYISDRFL PDKAIDLVDE AAAALAIQIG SVPVEIDQLE
     RRGTSLEIEK QALKRETDAA SRERMEIVER ELAEVQETAS GLRARWQTER GAIGKVAELK
     GRLESLRFQA EEETRRGNLQ RAAELQYGEI PQLERELKGL TEAQDELARV DSSHVSDARH
     GAPRASRMLK EEVDEEDIAA IVSRWTGIPV SKMLEGEVQK LVEMEARLRE RVVGQDEALS
     AVANAIRRSR AGLSDPKRPI GSFIFLGPTG VGKTETARAL AEFLFDDEAA MVRIDMSEYM
     EKHAVSRLIG APPGYVGYDE GGQLTEAVRR RPYGVVLFDE IEKAHPDVFN VLLQVLDDGR
     LTDSKGRTVD FKNTVLIMTS NIGAGQLSTA WAENEEGFED AKVRVIDSLK QHFRPEFLNR
     VDDIVVFHPL GEEQLAHIID LRLAELTQML ADRKIVIELT DEARAAIFKA GYDRAYGARP
     LKRAIQRMVQ DKLAIKILDG SVLHGDRVVV DAGRDGLTFS VSERVVSE
//
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