CLPB_STRAL
ID CLPB_STRAL Reviewed; 857 AA.
AC Q9Z6E4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB;
OS Streptomyces albus G.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=10027969; DOI=10.1046/j.1365-2958.1999.01193.x;
RA Grandvalet C., de Crecy-Lagard V., Mazodier P.;
RT "The ClpB ATPase of Streptomyces albus G belongs to the HspR heat shock
RT regulon.";
RL Mol. Microbiol. 31:521-532(1999).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=ClpB;
CC IsoId=Q9Z6E4-1; Sequence=Displayed;
CC Name=ClpB';
CC IsoId=Q9Z6E4-2; Sequence=VSP_018964, VSP_018988;
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:10027969}.
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; AF076980; AAD15989.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Z6E4; -.
DR SMR; Q9Z6E4; -.
DR PRIDE; Q9Z6E4; -.
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 Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 2: Evidence at transcript level;
KW Alternative initiation; ATP-binding; Chaperone; Coiled coil; Cytoplasm;
KW Nucleotide-binding; Repeat; Stress response.
FT CHAIN 1..857
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000005495"
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 5..72
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 56..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 160..341
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 342..546
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 556..762
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 763..857
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 392..525
FT /evidence="ECO:0000250"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 605..612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..149
FT /note="Missing (in isoform ClpB')"
FT /evidence="ECO:0000305"
FT /id="VSP_018964"
FT VAR_SEQ 150
FT /note="V -> M (in isoform ClpB')"
FT /evidence="ECO:0000305"
FT /id="VSP_018988"
SQ SEQUENCE 857 AA; 94150 MW; A9125DC49579F519 CRC64;
MDAELTNRSR DALNAATTRA VSAGNPDLTP AHLLLALLEG QDNENLVDLL AAVERRPGGG
SARAPSASLG SLPGVTGSTV APPQPNRDLL AVIADAGRRA KDLGDEFLST EHLLIGIRPT
ARPPRCSPGR APTPEKLLEA FQNTRGGRRV TTPRPEGQYK ALEKFGTDFT AAARERKLDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLKDKRLVS
LDLGAMVAGA KYRGEFEERL KTVLSEIKES DGQIVTFIDE LHTVVGAGAA DSAMDAGNML
KPMLARGELR MVGATTLDEY RERIEKDPAL ERRFQQVLVA EPSVEDSIAI LRGLKGRYEA
HHKVQIADSA LVAAATLSDR YITSRFLPDK AIDLVDEAAS RLRMEIDSSP LEIDELQRSV
DRLKMEELAL DRETDPASRQ RLEKLRRDLA DRERSCAAHR PWEKEKQSLN RVGELKERLD
ELRGQAERAQ QHGDFDTASK LLYGEIPTLE RDLRWRPAEE EAAKDTMVKE EVGPDDIADV
VGSWTGIPAG RLLEGETQKL LRMEAELGRR LIGQSEAVQA VSDAVRTRAG IADPDRPTGS
FLFLGPTGVG KTELAKALAD FLFDDERAMI RIDMSEYGEK HSVARLVGAP PGYVGYEEGG
QLTEAVRRRP YSVVLLDEVE KAHPGVFDIL LQVLDDGRLT DGQGRTVDFR NTILVLTSNL
GSQYLVGSAP EEEKRRQVME VVRSSFKPEF LNRLDDLVIF SALDEDELAR IAGLQIAGLA
RRLADRRLSL DVTPEALAWL AKEGFDPAYG ARPLRRLIQT AIGDRLAKEI LAGEVRDGDT
VRVDRVEDGL LVGRAEG
