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
//