ID CLPB2_STRAW Reviewed; 879 AA.
AC Q826F2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Chaperone protein ClpB 2;
GN Name=clpB2; OrderedLocusNames=SAV_7241;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC discriminating domain, recruiting aggregated proteins to the ClpB
CC hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC hexamer probably in an ATP-dependent manner. The movement of the
CC coiled-coil domain is essential for ClpB ability to rescue proteins
CC from an aggregated state, probably by pulling apart large aggregated
CC proteins, which are bound between the coiled-coils motifs of adjacent
CC ClpB subunits in the functional hexamer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; BA000030; BAC74952.1; -; Genomic_DNA.
DR RefSeq; WP_010988636.1; NZ_JZJK01000085.1.
DR AlphaFoldDB; Q826F2; -.
DR SMR; Q826F2; -.
DR KEGG; sma:SAVERM_7241; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_11; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
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; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..879
FT /note="Chaperone protein ClpB 2"
FT /id="PRO_0000191184"
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..71
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 86..151
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 164..345
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 346..553
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 563..775
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 776..879
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 396..530
FT /evidence="ECO:0000250"
FT BINDING 211..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 613..620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 879 AA; 98274 MW; 33C63069F68D6C47 CRC64;
MDMNRLTQKS QEALQEAQTA AGRMGHTEVD GEHLLLALLD QEDGLIPRLL QQAGTEPKEL
RAAVREELSH RPKATGPGAA PGQVFVTQRL ARLLDAAERE AKRLKDEYVS VEHLLLALAE
ESSSTAAGLL LKQAGITRDS FLSALTQVRG NQRVTSANPE VAYEALEKYG RDLVLEARSG
RLDPVIGRDA EIRRVTQILS RKTKNNPVLI GDPGVGKTAI VEGLAQRIVR GDVPEGLRDK
TVFALDMGSL VAGAKYRGEF EERLKAVLSE VKAAEGRILL FVDELHTVVG AGAAEGAMDA
GNMLKPMLAR GELHMIGATT LDEYRKHIEK DAALERRFQQ VLVDEPSVED TISILRGLRE
RLEVFHGVKI QDTALVSAAT LSHRYITDRF LPDKAIDLVD EACARLRTEI DSMPAELDEI
TRRVTRLEIE EAALSKESDP ASKTRLEELR RELADLRGEA DAKHAQWEAE RQAIRRVQEL
RQELEQVRHE AEEAERAYDL NRAAELRYGR LQDLERRLAA EEEQLAAKQG ENRLLREVVT
EEEIAEIVAA WTGIPVARLQ EGEREKLLRL DEILRERVIG QDEAVKLVTD AIIRARSGIR
DPRRPIGSFI FLGPTGVGKT ELAKTLARTL FDSEENMVRL DMSEYQERHT VSRLMGAPPG
YVGYEEGGQL TEAVRRKPYS VVLFDEIEKA HTDVFNTLLQ ILDDGRITDA QGRTVDFRNT
VIIMTSNIGS EHLLDGATAE GEIKPDARAL VMGELRGHFR PEFLNRVDDI VLFKPLGERQ
IERIVELQFD ELRQRLAERR ITVELTDAGR EVIAHQGYDP VYGARPLRRY ISHEVETLVG
RALLRGDVQD GATVRVDAEH GELVVTYDQP EDVKGAWAA
//
