ID E6U566_ETHHY Unreviewed; 872 AA.
AC E6U566;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Ethha_2380 {ECO:0000313|EMBL:ADU27879.1};
OS Ethanoligenens harbinense (strain DSM 18485 / JCM 12961 / CGMCC 1.5033 /
OS YUAN-3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ethanoligenens.
OX NCBI_TaxID=663278 {ECO:0000313|EMBL:ADU27879.1, ECO:0000313|Proteomes:UP000001551};
RN [1] {ECO:0000313|EMBL:ADU27879.1, ECO:0000313|Proteomes:UP000001551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18485 / JCM 12961 / CGMCC 1.5033 / YUAN-3
RC {ECO:0000313|Proteomes:UP000001551};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Wang A.,
RA Mouttaki H., He Z., Zhou J., Hemme C.L., Woyke T.;
RT "Complete sequence of Ethanoligenens harbinense YUAN-3.";
RL Submitted (DEC-2010) 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; CP002400; ADU27879.1; -; Genomic_DNA.
DR RefSeq; WP_013486225.1; NZ_CP025286.1.
DR AlphaFoldDB; E6U566; -.
DR STRING; 663278.Ethha_2380; -.
DR KEGG; eha:Ethha_2380; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_9; -.
DR Proteomes; UP000001551; 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:UP000001551};
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 414..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 97709 MW; 696BF967B89D4765 CRC64;
MTMEEFTVKA QEAISTSQEL AIRLGNQQVD GEHLHAALVQ QKDGLIPRLL GYMAVPLEQY
RAELDAQLDK LPRVSGGGAD QTYLTRRYST LLLHAQDESK KFKDEYTGVE HIYIALLKEK
GTPSEAVFRR FGVTLEKFME ALQKVRSNQR IESQDPEATY DSLKKYGRDL VEMAKAGKLD
PVIGRDAEIR RAIRILSRRT KNNPVLIGEP GVGKTAVVEG LAQRILKGDV PEGLRDKTIF
ALDLGALIAG AKFRGEFEER LKAVLKDVEK SDGRIILFID EIHTIVGAGK ADGAMDAGNL
LKPMLARGEL HCIGATTMDE YHKYIEKDAA LERRFQPIVV DQPSVEDTIS ILRGLKEKFE
IHHGVRITDG ALIACAELSD RYISDRFLPD KAIDLMDEAA AMLRTEIDSM PTELDEISRR
VMQLEIERQA LKKEDDPASQ SRLVTLEKEL AALKEKGDRM KAQWEMEKKD IGREKEIKQQ
IEDVKREIEE AERRYDLEKL AVLQNGKLPE LQKELEEEKK RVASAGGEHL LKEEVTEEEI
AEIVGKWTGI PVTRLVENER QKLLHLGDTL HRRVIGQDSA VEAVCDAVIR ARSGLKDPTK
PIGSFLFLGP TGVGKTELAK ALSEALFDSE NNVVRIDMSE YMEKFAVARL IGAPPGYVGY
EEGGQLTEAV RRKPYCVILF DEIEKAHPDV FNILLQLLDD GRLTDSQGRT VDFKNTVVIM
TSNLGSQYLL DGIRPDGSID SAAEEAVQRE LHLHFKPEFL NRIDETVLFK PLREEEIVRI
IDLALAGIQK RMDDHRWTLE VTDEAKKYMA AQSYTPAYGA RPVKRFMQKY VETAVGKKII
AGDVPDGATI HIGLKDGALD ISVRDPKPVA AG
//
