CLPB_HELHP
ID CLPB_HELHP Reviewed; 859 AA.
AC Q7VJY3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=HH_0109;
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1;
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(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; AE017125; AAP76706.1; -; Genomic_DNA.
DR RefSeq; WP_011114952.1; NC_004917.1.
DR AlphaFoldDB; Q7VJY3; -.
DR SMR; Q7VJY3; -.
DR STRING; 235279.HH_0109; -.
DR PRIDE; Q7VJY3; -.
DR EnsemblBacteria; AAP76706; AAP76706; HH_0109.
DR KEGG; hhe:HH_0109; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_7; -.
DR OMA; GPEHILM; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000002495; 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 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; 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 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..859
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191128"
FT DOMAIN 4..146
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 7..72
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 85..146
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 159..339
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 340..547
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 557..764
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 765..859
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 390..524
FT /evidence="ECO:0000250"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 607..614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 859 AA; 95301 MW; F0CB65059D07F7A3 CRC64;
MNLFEKLTNQ MKETLDSAAS LALHSSNQEI SLAHIYWALL SNHQSVLNQA LNKMNIDKTA
LELQARSEVD KLPKSSQVQK ENLSISKELS SALNLAQGEA IKNGDSFIAV DMFLIANLKE
STFVAIFKPL VDIAEFKKTL LSLRGESKIE SQSGDDNLES LSKFGIDLTQ KALENTLDPV
IGRDDEINAM MQILIRKSKN NPILLGEPGV GKTAVVEGLA QRIVAKAVPT SLQNKKLIAL
DMSALIAGAK YRGEFEERLK NVVDEVKKAG NIILFIDEIH TIVGAGASEG SMDAANILKP
ALARGELHTI GATTLKEYRK YFEKDAALTR RFQPINVNEP SINEALQILR GIKPNLEAHH
NVNITDAALV AAAKLSSRYI TDRFLPDKAI DLIDEAAAEL KMQIESEPLE LSKIKKHIAN
LEVEKQALNM EKTNVNEARV LEIDKELENL REEKMSLEGK FEQEKSVFTR IATIKAELDS
LKRESELAKR SGDYNKAAEI DYGKIPDIQA QEAALHKQWE EMQQNGTLLK NAVTQESIAG
VVSRWSGIPI KKMLQSQKER ILGIESELAK SVVGQDDAIK AIARAIKRNK AGLNDASRPI
GSFLFLGPTG VGKTQCAKTL AEFLFDNAKS LVRIDMSEYM EKHAVSRLVG APPGYVGYEE
GGVLTEAIRR KPYSIVLFDE VEKAHPDVFN ILLQVLDDGR LTDSKGVSVD FSNTIIILTS
NIASDKIMEI GDKQERQKAV KEALKMYFKP EFLNRLDDVV VFNPLGLADI TQIVDIMFKS
LAKRALEKGI NVTLSQEARE HIAQVGFDSV YGARPLKRAL YEEVEDRLAD LILRDEIKEG
DRVNFALKNG EICTHIEKE
