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Database: UniProt
Entry: A6LBC0_PARD8
LinkDB: A6LBC0_PARD8
Original site: A6LBC0_PARD8 
ID   A6LBC0_PARD8            Unreviewed;       862 AA.
AC   A6LBC0;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 118.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=BDI_1223 {ECO:0000313|EMBL:ABR42984.1};
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR42984.1, ECO:0000313|Proteomes:UP000000566};
RN   [1] {ECO:0000313|EMBL:ABR42984.1, ECO:0000313|Proteomes:UP000000566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC   {ECO:0000313|Proteomes:UP000000566};
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR42984.1; -; Genomic_DNA.
DR   RefSeq; WP_011966358.1; NC_009615.1.
DR   AlphaFoldDB; A6LBC0; -.
DR   STRING; 435591.BDI_1223; -.
DR   PaxDb; 435591-BDI_1223; -.
DR   KEGG; pdi:BDI_1223; -.
DR   PATRIC; fig|435591.13.peg.1203; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_10; -.
DR   OMA; SKMMQGE; -.
DR   BioCyc; PDIS435591:G1G5A-1258-MONOMER; -.
DR   Proteomes; UP000000566; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000000566};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          410..528
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   862 AA;  97061 MW;  7EE0ECC2DEDB2BC8 CRC64;
     MNLNNFTIKA QEAVQQAVQL VTKNNQQVIE PVHLLKAVIM TGESVTNFIF QKLGVNAQNL
     NMVLDRQIES YPKVSGGEPY LSSESNAVLQ KAIDYSSKMG DQYVSLEPII LALFTEKSTA
     SQILKDAGVT EKELRQAIEE LRKGNKVTSQ SAEETYDALG KYAINLNERA RSGKLDPVIG
     RDEEIRRVLQ ILSRRTKNNP ILIGEPGVGK TAIAEGLAHR IVRGDVPENL KSKQIFSLDM
     GALIAGAKYK GEFEERLKAV VNEVTKSEGE IILFIDEIHT LVGAGKGEGA MDAANILKPA
     LARGELRSIG ATTLDEYQKY FEKDKALERR FQTVIVDEPS ELDTISILRG LKEKYENHHK
     VRIKDDAIIS AVQLSTRYIT DRFLPDKAID LMDEAAARLR LQIDSVPESL DEVSRRIKQL
     EIEREAIKRE NDTSKLEQLN KEIADLKEEE TKQKAQWQSE KEQINKIQQN KIDIENLKFE
     ADKAEREGDY GKVAEIRYGK IKQKEEEIRE VQAKLKTMQG AAAMIKEEVD SDDIADVVSR
     WTGIPVSKMM QSEKDKLLRL ESELHTRVIG QEEAINAIAD AVRRSRAGLQ DPKRPIGSFI
     FLGTTGVGKT ELAKALAEYL FDDENMMTRI DMSEYQEKFS ATRLIGAPPG YVGYDEGGQL
     TEAIRRKPYS VVLFDEIEKA HPDVFNILLQ VLDDGRLTDN KGRVVNFKNT IIIMTSNLGS
     SLIRENFEKM TPATHDKVVD ETKIQVLELL KKTIRPEFLN RIDDIIMFTP LNEEEIRKIV
     SLQLSSVKKM LATNGVALDF TNEAVDFIAD KGFDPQFGAR PVKRVIQKYV LNELSKALLG
     GTVDRNRPIV IDRKDDGLEF KN
//
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