CLPB_WOLPM
ID CLPB_WOLPM Reviewed; 853 AA.
AC Q73IE4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=WD_0224;
OS Wolbachia pipientis wMel.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=163164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA O'Neill S.L., Eisen J.A.;
RT "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT streamlined genome overrun by mobile genetic elements.";
RL PLoS Biol. 2:327-341(2004).
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; AE017196; AAS13968.1; -; Genomic_DNA.
DR RefSeq; WP_010962444.1; NC_002978.6.
DR AlphaFoldDB; Q73IE4; -.
DR SMR; Q73IE4; -.
DR STRING; 163164.WD_0224; -.
DR PRIDE; Q73IE4; -.
DR EnsemblBacteria; AAS13968; AAS13968; WD_0224.
DR GeneID; 29555790; -.
DR KEGG; wol:WD_0224; -.
DR eggNOG; COG0542; Bacteria.
DR OMA; ERMKAVM; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000008215; 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 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; Repeat;
KW Stress response.
FT CHAIN 1..853
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191204"
FT DOMAIN 3..148
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 84..148
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 161..342
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 343..544
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 554..760
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 761..853
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 393..524
FT /evidence="ECO:0000250"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 604..611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 853 AA; 94859 MW; 46B5006F9AD13F09 CRC64;
MDLNKFTEKA KSLIQSAQMK ALGAGHQIFM PEHLLKVMLE DESGLVQDLI NACGGNVQSI
SDAVDSAIKK LPVIEGPGSG GLQLSREIAK VFEDSIGIAK RNKDSFVAVE RLLQGLTAQK
DDTVGKILAE NGVTPQKLNS VVAEMRKGSS ADSPNSEEKL NAAKKYTKDV TELAMQGKLD
PVIGRDEEIR RTMQVSLRRT KNNPVLIGEP GVGKTAIVEG LANRIVANDV PLGLHDAKVL
ALDLGALIAG TKFRGEFEER LKAVINELSR AEGKVILFID ELHTLVGAGA TSGAMDASNL
LKPALARGEV RCIGATTLDE YRQHIEKDPA LARRFQPVFI SQPTETDTIS ILRGLKERYE
VHHGIRITDG AIIAAATLSN RYITDRFLPD KAIDLIDEAA SRVRIEMDSK PEVIDELERK
VIQLKIEAEA LKKESDENSK QRLKKINEEI ENLNSKFADL NSKWQMEKNK IARIQETAEK
LDNARKELEL VQRSGNLGRA GELMYGVIPQ LENELKNQEK VTDSFLKKEV TGDDIANIVS
KWTGIPVDNM MHSEKEKLLN MENEIGRRVI GQKDAIEAIS NAVRRSRSGV QDTNKPFGSF
LFLGPTGVGK TELAKALAEF LFDDQSALLR FDMSEYMEKH SVSKLIGAPP GYVGYEQGGR
LTEAVRRRPY QVILFDEIEK ANPDIFNLLL QILDEGRLTD SHGKLIDFRN TILILTSNLG
AEIMLKGNVD SVRNEVMQIV KSAFRPEFLN RLDEIIIFHS LTRDDIYKII DVQFSYLQKT
LAKRKLSISL LQEAKELIAQ TGYDPEYGAR PLKRVIQECI QNNLAKLVLS GEVVENDELI
VYALDNEILV KKV
