CLPB_TREPA
ID CLPB_TREPA Reviewed; 878 AA.
AC O83110;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=TP_0071;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC65062.1; -; Genomic_DNA.
DR PIR; G71371; G71371.
DR RefSeq; WP_010881520.1; NC_021490.2.
DR AlphaFoldDB; O83110; -.
DR SMR; O83110; -.
DR IntAct; O83110; 5.
DR STRING; 243276.TPANIC_0071; -.
DR EnsemblBacteria; AAC65062; AAC65062; TP_0071.
DR GeneID; 57878611; -.
DR KEGG; tpa:TP_0071; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_12; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000000811; 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..878
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191197"
FT DOMAIN 3..146
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 83..146
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 159..340
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 341..549
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 559..783
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 784..878
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 391..525
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 609..616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 878 AA; 98981 MW; 7D9E7419E42A2202 CRC64;
MNTDRYTVKA SEALNDAISL AEAENHGQVE EEHLLHALLS QKDGIISPLI EKIGAKPDFL
YDELLQCLRR KPRVTGPAAQ TRCAPTLSKA CARAERLALK NQDEYVSCEH LLLAISETDS
NTARLLHSQG ITSKTISAAL KDIRGSKRVT SQDPESTFQC LEKYCRDLTT LAREEKIDPV
IGRDEEIRRV MQVLSRRTKN NPVLIGEPGV GKTAIVEGLA RRIVSGDVPE SLKGKRLLSL
DLGALVAGAK FRGEFEERLK AVIEAVQKSD GGVILFIDEL HTLVGAGASE GSMDASNLLK
PALARGELRS IGATTLNEYR KYIEKDAALE RRFQQVYCVQ PTVEDTIAIL RGLQEKYEVH
HGVRIKDEAL VAATVLSDRY ITNRFLPDKA IDLVDEAASR LKMEIESQPV ELDQVERKIL
QLNIEKASLL KESDPASKER LEKLEKELAG FLERRAAMQV QWQNEKGRIE ESRRYKEELE
RLRIEETMFS REGDLNKAAE LRYGKIPELE KKIMLLTAEV EKKSGLEGQL LREEVCEEDI
AKIISMWTGI PVSKMMASEQ QKYLQLESVL MQRVVGQDEA VRVISDAIRR NKAGLSDTRR
PLGSFLCVGP TGVGKTELAR TLADFLFNDE RALTRIDMSE YMEKHAISRL IGAPPGYVGY
DEGGQLTEAV RRRPYSVLLF DEVEKAHQDV FNIFLQILDD GRLTDGQGRV VDFRNTIIIM
TSNIGSEHIL SARESRTHTS DLPVPETQST EEQTLPEQIR GLLHTYFRPE FLNRIDEVLI
FKRLTRKHIR LITDIQLQMV VERLESRHIK LRVRDAAKAY LAERGYDDTF GARPLKRAIQ
TELENALARE ILSGRFRGGS TIVVDMCKDA LCFTEQTS
