CLPB_FUSNN
ID CLPB_FUSNN Reviewed; 857 AA.
AC Q8RHQ8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=FN1941;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAL94040.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009951; AAL94040.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_602741.1; NC_003454.1.
DR AlphaFoldDB; Q8RHQ8; -.
DR SMR; Q8RHQ8; -.
DR STRING; 190304.FN1941; -.
DR PRIDE; Q8RHQ8; -.
DR EnsemblBacteria; AAL94040; AAL94040; FN1941.
DR KEGG; fnu:FN1941; -.
DR PATRIC; fig|190304.8.peg.416; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_0; -.
DR InParanoid; Q8RHQ8; -.
DR OMA; SKMMQGE; -.
DR Proteomes; UP000002521; 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 GO; GO:0042026; P:protein refolding; 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..857
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191123"
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 85..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..546
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 556..764
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 765..857
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 606..613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 857 AA; 97405 MW; 22614869B73A64E0 CRC64;
MNPNQFTENT ISAINLAVDI SKGNMQQSIK PEALALGLLM QNNGLIPRVI EKMGLNLQYI
ISELEKEMNN YPKVEVKVSN ENISLDQKTN SILNRAEKIM NEMEDSFLSV EHIFKAMIEE
MPIFKRFGIS LEKYMEVLMN IRGNRKVDNQ NPEATYEVLE KYAKDLVELA REGKIDPIIG
RDSEIRRAIQ IISRRTKNDP ILIGEPGVGK TAIVEGLAQR ILNGDVPESL KNKKIFSLDM
GALVAGAKYK GEFEERMKGV LKEVEESNGN IILFIDEIHT IVGAGKGEGS LDAGNMLKPM
LARGELRVIG ATTIDEYRKY IEKDPALERR FQTILVNEPN VDDTISILRG LKDKFETYHG
VRITDTAIVE AATLSQRYIS DRKLPDKAID LIDEAAAMIR TEIDSMPEEL DQLTRKALQL
EIEIKALEKE TDDASKERLK VIEKELAELN EEKKVLTSKW ELEKEDISKI KNIKREIENV
KLEMEKAERE YDLTKLSELK YGKLATLEKE LQEQQNKVDK DGKENSLLKQ EVTADEIADI
VSRWTGIPVS KLTETKKEKM LHLEDHIKER VKGQDEAIKS VADTMLRSVA GLKDPNRPMG
SFIFLGPTGV GKTYLAKTLA YNLFDSEDNV VRIDMSEYMD KFSVTRLIGA PPGYVGYEEG
GQLTEAIRTK PYSVILFDEI EKAHPDVFNV LLQVLDDGRL TDGQGRIVDF KNTLIIMTSN
IGSHFILEDP NLSEDTREKV ADELKARFKP EFLNRIDEII TFKALDLPAI KEIVKLSLKD
LENKLKPKHI TLEFSDKMVD YLANNAYDPH YGARPLRRYI QREIETSLAK KILANEVHEK
SNVLIDLDNN HIVFKEV
