ID B7ASX2_9FIRM Unreviewed; 864 AA.
AC B7ASX2;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BACPEC_02180 {ECO:0000313|EMBL:EEC57668.1};
OS [Bacteroides] pectinophilus ATCC 43243.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=483218 {ECO:0000313|EMBL:EEC57668.1, ECO:0000313|Proteomes:UP000003136};
RN [1] {ECO:0000313|EMBL:EEC57668.1, ECO:0000313|Proteomes:UP000003136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC57668.1,
RC ECO:0000313|Proteomes:UP000003136};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides pectinophilus (ATCC 43243).";
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEC57668.1, ECO:0000313|Proteomes:UP000003136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC57668.1,
RC ECO:0000313|Proteomes:UP000003136};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2008) 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. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; ABVQ01000036; EEC57668.1; -; Genomic_DNA.
DR AlphaFoldDB; B7ASX2; -.
DR STRING; 483218.BACPEC_02180; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_9; -.
DR Proteomes; UP000003136; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 407..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 864 AA; 96814 MW; 148BBE8392C4D878 CRC64;
MNINKFTQKS MEAVQGCEKL AYEYGNQEID QEHFLYSLLN IEDSLIAGLI EKMGIDRNAF
TRDVEALIQK KPKVSGSGAG QVYVSNALNK VLISAEDVAK QMGDSYVSVE HLFIALLNEP
NRDVKELFKR YNVTKDGFLK ALSTVRGNQK VTTDNPEATY DTLKKYGQDL VEKARDGKMD
PVIGRDNEIR NVIRILSRKT KNNPVLIGEP GVGKTAVVEG LAQRIVRGDV PEGLKDKKLF
ALDMGALVAG AKYRGEFEER LKAVLDEVKK SEGQIILFID EIHTIVGAGK TEGAMDAGNM
LKPMLARGEL HCIGATTLDE HREYIEKDPA LERRFQPVMV DEPSVEDTIS ILRGLKDRYE
VYHGVKITDG ALVSAATLSD RYISDRYLPD KAIDLVDEAC AMIKTELDSM PAELDEMQRK
IMQLEIEEQA LKKEEDNLSR ERLDSLQKEL AQLREEFSQQ KQKWDSEKSS VDKISKLKEE
IDHVNQEIQN AKSDYNLEKA AELQYGRLPE LTKQLNEAEE KAHSKDMQLI HESVTEDEIA
KIVSRWTGIP VARLSETERQ KTLKLDELLH RRVVGQDEGV TKVTEAIIRS KAGIKDPTKP
IGSFLFLGPT GVGKTELAKA LAESLFDDES NIVRLDMSEY MEKYSVSRLI GAPPGYVGYD
EGGQLTEAVR RKPYSVVLFD EVEKAHPDVF NVLLQVLDDG RITDSQGRTV DFKNTIIIMT
SNIGSQYLLD GIDADGNISS DAENAVMGDL RNHFRPEFLN RLDEIIMFKP LTKSNISSII
DLLIKDVNKR LADKELTVKL TDAARDFIVD NGFDPMYGAR PLKRYVQKTV ETLAAKLILA
GNIDAQSVIL IDVEDGKLTA RAEK
//