CLPB_HELPY
ID CLPB_HELPY Reviewed; 856 AA.
AC P71404;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=HP_0264;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RX PubMed=9440536; DOI=10.1128/jb.180.2.426-429.1998;
RA Allan E., Mullany P., Tabaqchali S.;
RT "Construction and characterization of a Helicobacter pylori clpB mutant and
RT role of the gene in the stress response.";
RL J. Bacteriol. 180:426-429(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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 Necessary for surviving high-temperature stress. {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; Y08238; CAA69406.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07330.1; -; Genomic_DNA.
DR PIR; H64552; H64552.
DR RefSeq; NP_207062.1; NC_000915.1.
DR RefSeq; WP_001048043.1; NC_018939.1.
DR AlphaFoldDB; P71404; -.
DR SMR; P71404; -.
DR DIP; DIP-3665N; -.
DR IntAct; P71404; 1.
DR MINT; P71404; -.
DR STRING; 85962.C694_01335; -.
DR PaxDb; P71404; -.
DR EnsemblBacteria; AAD07330; AAD07330; HP_0264.
DR KEGG; hpy:HP_0264; -.
DR PATRIC; fig|85962.47.peg.284; -.
DR eggNOG; COG0542; Bacteria.
DR OMA; ERMKAVM; -.
DR PhylomeDB; P71404; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
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..856
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191130"
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"
FT CONFLICT 14
FT /note="T -> A (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="M -> L (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="Q -> E (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="R -> K (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="S -> N (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="R -> T (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="G -> S (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="A -> T (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="R -> A (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="D -> G (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="M -> V (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="A -> H (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="V -> A (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 643..644
FT /note="MS -> IT (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="A -> P (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="E -> D (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="D -> G (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="V -> I (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="D -> G (in Ref. 1; CAA69406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 856 AA; 96684 MW; E3902C7D989496AD CRC64;
MNLFEKMTDQ LHETLDSALA LALHHKNAEV TPMHMLFAML NNSQGILIQA LQKMPVDIQA
LRLSVQSELN KFAKVSQISK QNIQLNQALI QSLENAQGLM AKRGDSFIAT DVYLLANMGL
FESVLKPYLD AKELQKTLES LRKGRTIQDK NDDSNLESLE KFGIDLTQKA LENKLDPVIG
RDEEIIRMMQ ILIRKTKNNP ILLGEPGVGK TAVVEGLAQR IMNKEVPKTL LNKRVIALDL
SLLVAGAKYR GEFEERLKKV IEEVKKSANV ILFIDEIHTI VGAGASEGGM DAANILKPAL
ARGELHTIGA TTLKEYRKYF EKDMALQRRF QPILLNEPSI NEALQILRGL KETLETHHNI
TINDSALIAS AKLSSRYITD RFLPDKAIDL IDEGAAQLKM QMESEPAKLS SVKRSIQRLE
MEKQALEMEK KESNAKRMQE ILKELSDLKE EKIQLEAQFE NEKEVFKEIS RLKMEMESLK
KEAERFKRNG DYQQAGEIEY SKIPENKKKE EELQRKWEAM QQNGALLQNA LTENNIAEIV
SQWTHIPVQK MLQSEKNRVL NIESELQKRV VGQEKAIKAI AKAIKRNKAG LSDSNKPIGS
FLFLGPTGVG KTESAKALAQ FLFDSDKNLI RIDMSEYLEK HAMSRLIGAA PGYVGYEEGG
QLTEAVRRKP YSVVLLDEVE KAHPDVFNLL LQVLDEGHLT DSKGVRVDFK NTILILTSNV
ASGALLEENL SEAEKQKAIK ESLRQFFKPE FLNRLDEIIS FNALDSHAVI NIVGILFENI
QKKALERGIN ITLDEEAKEL IAEAGFDRFY GARPLKRALY EMVEDKLAEL ILEDKVKEND
SVAFVVENNE IVPKIK
