CLPB_STRCO
ID CLPB_STRCO Reviewed; 865 AA.
AC Q8CJV9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=SCO3661; ORFNames=SCH10.39c, SCH44.01c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939117; CAD55328.1; -; Genomic_DNA.
DR PIR; T36551; T36551.
DR RefSeq; NP_733613.1; NC_003888.3.
DR RefSeq; WP_003975278.1; NZ_VNID01000003.1.
DR AlphaFoldDB; Q8CJV9; -.
DR SMR; Q8CJV9; -.
DR STRING; 100226.SCO3661; -.
DR PRIDE; Q8CJV9; -.
DR GeneID; 1099097; -.
DR KEGG; sco:SCO3661; -.
DR PATRIC; fig|100226.15.peg.3720; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_11; -.
DR InParanoid; Q8CJV9; -.
DR OMA; SKMMQGE; -.
DR PhylomeDB; Q8CJV9; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..865
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191185"
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 5..71
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 84..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 160..342
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 343..549
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 559..767
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 768..865
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 393..527
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 609..616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 865 AA; 94438 MW; 4CBD714C9C0975A3 CRC64;
MDAELTNRSR DAINAASNRA VTEGNADLTP AHLLLALLQG QDNENITDLL AAVEADLAAV
RTGAERIVAG LPSVTGSTVA PPQPSREMLA VVADAQARAK ELGDEYLSTE HLLLGIAAKG
GAAGEVLEGQ GASAKKLQEA FRKARGGRRV TTADPEGQYK ALEKFGTDLT AAARDGKLDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLKDKRLVA
LDLGAMVAGA KYRGEFEERL KTVLAEIKDS DGQVVTFIDE LHTVVGAGAG GDSAMDAGNM
LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVLV AEPTVEDSIA ILRGLKGRYE
AHHKVQIADS ALVAAASLSD RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PVEIDELQRS
VDRLKMEELA IGKETDAASL ERLERLRRDL ADKEEELRGL TARWEKEKQS LNRVGELKEK
LDELRGQAER AQRDGDFDTA SKLLYGEIPD LERDLEAASE AEEEVARDTM VKEEVGADDI
ADVVASWTGI PAGRLLEGET QKLLRMEDEL GKRLIGQTQA VRAVSDAVRR SRAGIADPDR
PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMVRIDMSE YSEKHSVARL VGAPPGYVGY
EEGGQLTEAV RRRPYTVVLL DEVEKAHPEV FDILLQVLDD GRLTDGQGRT VDFRNTILVL
TSNLGSQYLV DPTTGEAEKK QQVLEVVRSS FKPEFLNRLD DLVVFSALSQ EELSRIARLQ
INGLARRLAE RRLTLEVTDE ALAWLAEEGN DPAYGARPLR RLVQTAIGDR LAREILSGEI
KDGDTVRVDR FGDELIVGPA SGKTL
