CLPB_BORPE
ID CLPB_BORPE Reviewed; 865 AA.
AC Q7VYV6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=BP1198;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(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; BX640414; CAE41494.1; -; Genomic_DNA.
DR RefSeq; NP_879972.1; NC_002929.2.
DR RefSeq; WP_010930242.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VYV6; -.
DR SMR; Q7VYV6; -.
DR STRING; 257313.BP1198; -.
DR PRIDE; Q7VYV6; -.
DR KEGG; bpe:BP1198; -.
DR PATRIC; fig|257313.5.peg.1290; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_4; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000002676; 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;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..865
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191097"
FT DOMAIN 3..145
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 82..145
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 158..339
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 340..551
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 561..770
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 771..865
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 390..524
FT /evidence="ECO:0000250"
FT BINDING 205..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 611..618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 865 AA; 96334 MW; A3CED31F9D10FFDF CRC64;
MRFDKLTTKF QQALADAQSL AARNDHPYIE PVHVLAALLG DPDSGAASLL ARAGVAVNRV
QPAIDSALKG LPQVQGDDNV QVGRELQSVL VRTDKEAARR GDTYIASELF LLALADDKGD
AGRILREAGL QKKALEAAID AVRGGENVSG AEGESNREAL SKYTLDLTER ARQGKLDPVI
GRDDEIRRTI QILQRRTKNN PVLIGEPGVG KTAIVEGLAQ RIVNDEVPET LRGKRVLSLD
LAALLAGAKF RGEFEERLKA VLKELAQDDG QNIVFIDELH TMAGAGKAEG AMDAGNMLKP
ALARGELHCI GATTLDEYRK YIEKDAALER RFQKVLVGEP DVESTIAILR GLQERYELHH
GVEITDPAIV AAAELSHRYI TDRFLPDKAI DLIDEAGARI RMEIDSKPEV MDRLDRRIIQ
LKIEREAVKK ETDDASMRRL AVIEEELEKL QREYNDYEEI WKAEKAAVQG TQAIKEEIDR
VRAEMAELQR KGQFDKLAEL QYGKLPELEA RLKAADSAER EAGESDSGKP RLLRTQVGAE
EIAEVVSRAT GIPVAKMMQG ERDKLLRMED FLHKRVVGQD EAVRLVSDAI RRSRAGLADP
SRPYGSFLFL GPTGVGKTEL TRALADFLFD SEEHMIRIDM SEFMEKHSVA RLIGAPPGYV
GYEEGGYLTE AVRRKPYSVI LLDEVEKAHP DVFNVLLQVL DDGRLTDGQG RTVDFRNTVI
VMTSNLGSQH IQSMAGKPYE VIKEVVWDEL KHTFRPEFLN RIDEVVVFHG LEAQHIESIA
RIQLKRLGER LEKQEMRLDV SDAALAEIAR SGFDPVFGAR PLKRAIQQQI ENPVAKLILE
GVFGPRDVVP VDWQDGKFVF TRTLQ
