CLPB_BACAN
ID CLPB_BACAN Reviewed; 866 AA.
AC Q81TT4; Q6I218; Q6KVV5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=BA_1177, GBAA_1177, BAS1090;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) 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; AE016879; AAP25141.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT30265.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53413.1; -; Genomic_DNA.
DR RefSeq; NP_843655.1; NC_003997.3.
DR RefSeq; WP_000365381.1; NZ_WXXJ01000044.1.
DR RefSeq; YP_027362.1; NC_005945.1.
DR AlphaFoldDB; Q81TT4; -.
DR SMR; Q81TT4; -.
DR IntAct; Q81TT4; 26.
DR STRING; 261594.GBAA_1177; -.
DR DNASU; 1086217; -.
DR EnsemblBacteria; AAP25141; AAP25141; BA_1177.
DR EnsemblBacteria; AAT30265; AAT30265; GBAA_1177.
DR GeneID; 45021187; -.
DR KEGG; ban:BA_1177; -.
DR KEGG; bar:GBAA_1177; -.
DR KEGG; bat:BAS1090; -.
DR PATRIC; fig|198094.11.peg.1157; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_9; -.
DR OMA; GPEHILM; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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..866
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191088"
FT DOMAIN 3..149
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 86..149
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 162..343
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 344..551
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 561..773
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 774..866
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 394..528
FT /evidence="ECO:0000250"
FT BINDING 209..216
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 866 AA; 97545 MW; F4B6B1CA37081F93 CRC64;
MDLNQMTTKT QEAIMSAQSL AVSHHHQEVD TVHLLFTLLE EQDGLAVRIF QKMNVDIEAL
KQGVENLIKK KPSVTGSGAE AGKLYITGAL QQLLVRAGKE AEKLQDDYIS VEHVLLAFTE
EKGDISQLFT RFHITKDNLL QSLMTVRGNQ RVTSQNPEAT YEALEKYGRD LVAEVKAGKI
DPVIGRDSEI RRVIRILSRK TKNNPVLIGE PGVGKTAIVE GLAQRIVKKD VPEGLKDRTI
FALDMSALVA GAKFRGEFEE RLQAVLNEIK KSEGRILLFI DELHTIVGAG KTEGAMDAGN
MLKPMLARGE LHCIGATTLD EYRKYIEKDP ALERRFQQVL AEEPTVEDTI SILRGLKERF
EIYHGVNIHD RAIVAASVLS DRYISDRFLP DKAIDLVDEA CATIRTEIDS MPTELDEVTR
RIMQLEIEEA ALGKEKDFGS QERLKTLQRE LSDLKEVASS MRAKWEKEKE DIHKVRDLRE
HLERLRRELE EAEGNYDLNR AAELRHGKIP AIEKELKEAE EMGANNKQEN RLLREEVSEE
EIADIVSRWT GIPVAKLVEG EREKLLRLEQ ILSERVIGQE EAVSLVSDAV LRARAGIKDP
NRPIGSFIFL GPTGVGKTEL AKTLAQSLFD SEEQMIRIDM SEYMEKHAVS RLIGAPPGYV
GYEEGGQLTE AVRRKPYSVI LLDEIEKAHP EVFNILLQML DDGRITDSQG RTVDFKNTVI
IMTSNIGSAH LLDGLEEDGS IKEESRELVM GQLRGHFRPE FLNRVDEIIL FKPLTTNEIK
GIVDKIVKEL QGRLADRHIT VKLTEAAKEF VVEAGFDPMY GARPLKRYVQ RQVETKLARE
LIAGTITDNS HVVVDVENNE LVVHVK
