CLPB_HELPJ
ID CLPB_HELPJ Reviewed; 856 AA.
AC Q9ZMH1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=jhp_0249;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD05825.1; -; Genomic_DNA.
DR PIR; C71956; C71956.
DR RefSeq; WP_001047947.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZMH1; -.
DR SMR; Q9ZMH1; -.
DR STRING; 85963.jhp_0249; -.
DR EnsemblBacteria; AAD05825; AAD05825; jhp_0249.
DR KEGG; hpj:jhp_0249; -.
DR PATRIC; fig|85963.30.peg.765; -.
DR eggNOG; COG0542; Bacteria.
DR OMA; GPEHILM; -.
DR Proteomes; UP000000804; 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; Repeat;
KW Stress response.
FT CHAIN 1..856
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191129"
FT DOMAIN 4..144
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..144
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 157..337
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 338..545
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 555..763
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 764..856
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 388..522
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; 96731 MW; 0B66658F6946588A CRC64;
MNLFEKMTDQ LHETLDSAIA LALHHKNAEV TPMHMLFAML NNSQGILIQA LQKMPVDIEA
LKLSVQSELN KFAKVSQISK QNIQLNQALI QSLENAQGLM AKRGDSFIAT DAYLLANMNL
FESVLKPYLD TKELQKTLES LRKGRTIQDK NDDSNLESLE KFGIDLTQKA LENKLDPVIG
RDEEIIRMMQ ILIRKTKNNP ILLGEPGVGK TAVVEGLAQR IVNKEVPKTL LNKRVVALDL
SLLVAGAKYR GEFEERLKKV IEEVKKSANV ILFIDEIHTI VGAGASEGGM DAANILKPAL
ARGELHTIGA TTLKEYRKYF EKDMALQRRF QPILLNEPSI NEALQILRGL KETLETHHNI
TINDSALIAS AKLSSRYITD RFLPDKAIDL IDEGAAQLKM QMESEPAKLS SVKRSIQRLE
MEKQALEMEN KESNHKRMQE ILKELSDLKE EKIQLEAQFE NEKEVFKEIS RLKMEMEGLK
KEAERFKRNG DYQQAAEIEY SKIPEKEKKE KELQHKWETM QQNGALLQNA LTENNIAEIV
SQWTHIPVQK MLQSEKNRVL NIESELQKRV VGQEKALKAI AKAIKRNKAG LSDSNKPIGS
FLFLGPTGVG KTESAKALAQ FLFDSDKNLI RIDMSEYMEK HAISRLIGAA PGYVGYEEGG
QLTEAVRRKP YSVVLLDEVE KAHPDVFNLL LQVLDEGHLT DSKGVRVDFK NTILILTSNV
ASGALLEEDL SEADKQKAIK ESLRQFFKPE FLNRLDEIIS FNALDSHAII NIVGILFENV
QKKALERGIN ITLDEKAKEL IAEAGFDRFY GARPLKRALY EMVEDKLAEL ILEDKIKEND
SVAFVVENNE IVPKIK
