ID L0A4A5_DEIPD Unreviewed; 852 AA.
AC L0A4A5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Deipe_3223 {ECO:0000313|EMBL:AFZ68666.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ68666.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-2012) 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; CP003382; AFZ68666.1; -; Genomic_DNA.
DR RefSeq; WP_015236964.1; NC_019793.1.
DR AlphaFoldDB; L0A4A5; -.
DR STRING; 937777.Deipe_3223; -.
DR KEGG; dpd:Deipe_3223; -.
DR PATRIC; fig|937777.3.peg.3239; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000010467; 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 78, MITOCHONDRIAL; 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:UP000010467};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..156
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 403..430
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 463..524
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 852 AA; 94328 MW; E4F2F74AF0A8BBCB CRC64;
MNPDRFTEAA LQAFTDAQAS AQGRGHQQLM PAHLLLASLT VNSPAARALA LAGGELGAAR
SALEAELAKL PRVQGSDNMY VDASVMRAVN AAEELARQFG DSFVGLDTLF LAIRQVYKGP
GLPDERAFRQ AIEQQRGGKK VDSKTAEQSF DALQKFGLDL TERAREGKLD PVIGRDEEIR
RTMQILLRRT KNNPVLIGEP GVGKTAIAEG LAARIVKGDV PEGLRNKRIV TLQMGSLLAG
AKYRGEFEER LKGVIQEVVD SAGEVILFID EIHTIVGAGK AEGAVDAGNM LKPALARGEL
HLIGATTLDE YREIEKDAAL ERRFQPVMVE EPSVEDTISI LRGIKERYQL HHNVEITDPA
LVAAATLSQR YIADRQLPDK AIDLIDEAAA RLRMALESSP EQIDALERRK LQLEIERQAL
SKEKDEDSQQ RLIDIEDSLR AVTDELGSLR GKWEAERHEL HDLRTKREQL DSVRTQIEQA
ERDYDLSKAA ELRYGQLPQL EREVQDLEAR LKNAEFAHQE VTDEDIAAIV ARWTGIPVSR
LMEGEREKLL RLEQELHRRV IGQHRAIVSV ADAIRRSRAG LSDPRRPIGS FMFLGPTGVG
KTELAKALAA FLFDTEDAMV RLDMSEYMEK HTVARLIGAP PGYVGYEEGG QLTEAVRRRP
YSVILLDEIE KAHPDVFNVL LQVLDDGRLT DGQGRTVDFR NSLVIMTSNI GSPLILEAQA
RGDDAETIRS AVMGALSQAF RPEFLNRVDD IIVFDALTSA DLHQIVDIQL RGLRERLAER
RVTLHLTDAA VNHLAAVGYD PNFGARPLKR AIGREIETPL AREILSGKLP DGSALTLDYQ
GGHLVFESAL VN
//
