CLPB_HAEDU
ID CLPB_HAEDU Reviewed; 856 AA.
AC Q7VNH1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=HD_0565;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017143; AAP95500.1; -; Genomic_DNA.
DR RefSeq; WP_010944553.1; NC_002940.2.
DR AlphaFoldDB; Q7VNH1; -.
DR SMR; Q7VNH1; -.
DR STRING; 233412.HD_0565; -.
DR PRIDE; Q7VNH1; -.
DR EnsemblBacteria; AAP95500; AAP95500; HD_0565.
DR KEGG; hdu:HD_0565; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_6; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000001022; 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..856
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191126"
FT DOMAIN 3..144
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..144
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 157..338
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 339..545
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 555..764
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 765..856
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 389..523
FT /evidence="ECO:0000250"
FT BINDING 204..211
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"
SQ SEQUENCE 856 AA; 95859 MW; 2B8CBEE2201888F9 CRC64;
MNFEKFTTKL QEALNEAQSL AVAKDNAYIE PVHLLYALVK QQDGAIAPLF TTLNVSTQTL
INELELILNQ LPQVTGTTTQ ASQQLIRLLN QTAKLAQQFN DSFISSELFL LAALDDHGSL
GKLFKAFGLT KENVTQAISQ MRGGESVNNQ NAEQTRQALQ KYTIDLTERA KTGKLDPVIG
RDEEIRRTVQ VLQRRTKNNP VLIGEPGVGK TAIVEGLAQR IVNGEVPEGL KNKRVLSLDM
GALIAGAKYR GEFEERLKAV LNELAKEEGQ VILFIDEIHT MVGAGKTDGA MDAGNLLKPS
LARGELHCVG ATTLDEYRQY IEKDAALERR FQKVLVDEPS VEDTIAILRG LKERYEIHHH
VQITDPAIVA AATLSHRYIS DRQLPDKAID LIDEAASSLR MEIDSKPEPL DKLERRIIQL
KLERQALQKE KDEASRQRLA KLDEEMTAKA QEYSALEEVW KAEKSALLGT QHLKTELENA
RIAMDQAKRA DNFEKMSELQ YGTIPALEKQ LQDAIKREEE NNDHHLLRTK VTEEEIAEVL
SKATGIPITK MMEGEKEKLL RMEQVLHSRV IGQNEAVEAV ANAILRSRAG LADPNKPIGS
FLFLGPTGVG KTELSKTLAN FLFDDENAIV RIDMSEFMEK HSVSRLVGAP PGYVGYEQGG
YLTEAVRRRP YSVVLLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
GAHLIQENAE ITYLAMKEMV MSVVSQHFRP EFINRIDETV VFHPLDQQHI RAIANIQLQR
LIRRLAERGY QVTISDTALD HISQAGFDSL FGARPLKRAI QQELENPLAQ QILSGKLLPN
NPVIIDYQDN HIIAKQ
