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Database: UniProt
Entry: B7ASX2_9FIRM
LinkDB: B7ASX2_9FIRM
Original site: B7ASX2_9FIRM 
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
//
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