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Database: UniProt
Entry: A0A087AIG8_9BIFI
LinkDB: A0A087AIG8_9BIFI
Original site: A0A087AIG8_9BIFI 
ID   A0A087AIG8_9BIFI        Unreviewed;       899 AA.
AC   A0A087AIG8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BCUN_1746 {ECO:0000313|EMBL:KFI58568.1};
OS   Bifidobacterium cuniculi.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1688 {ECO:0000313|EMBL:KFI58568.1, ECO:0000313|Proteomes:UP000029067};
RN   [1] {ECO:0000313|EMBL:KFI58568.1, ECO:0000313|Proteomes:UP000029067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 10738 {ECO:0000313|EMBL:KFI58568.1,
RC   ECO:0000313|Proteomes:UP000029067};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFI58568.1}.
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DR   EMBL; JGYV01000029; KFI58568.1; -; Genomic_DNA.
DR   RefSeq; WP_034258676.1; NZ_JGYV01000029.1.
DR   AlphaFoldDB; A0A087AIG8; -.
DR   STRING; 1688.BCUN_1746; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000029067; 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   Reference proteome {ECO:0000313|Proteomes:UP000029067};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          864..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          399..493
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   899 AA;  98474 MW;  469342B51C02572B CRC64;
     MEQKFTTLAQ EALGDAIQSA SAAGNPQVDP LHLLDALLRQ QNGVIRGLVE QCGGNVQTIG
     AAVRNALVAL PSASGSSTAQ PQASRQLTQA IVEAEKAMKE MGDEYVSTEH LLLGIVEAKP
     NEAAKILEAN GVTAEKIRKA IPEVRGGAKV TSPDAEASYK ALEKFSTDLT QRAKDGKLDP
     VIGRDQEIRR VIQILSRRTK NNPVLIGEPG VGKTAVVEGL AERIVAGDVP STLQNKRLIS
     LDLGSMVAGS KYRGEFEERL KSVLDEIRQS DGQIITFIDE LHTIVGAGAA EGSMDAGNML
     KPMLARGELR LIGATTLDEY RENIEKDPAL ERRFQQVYVG EPSVEDTVAI LRGLKQRYEA
     HHKVTIGDDA LVAAATLSNR YITGRQLPDK AIDLVDEAAA HLRMELDSQP EEIDELQRKV
     TRLEMEEMQL KKAEDAASKD RLAKLQSELA DAREQLAGLK ARWDAEKAGH NKVGDLRAKL
     DEKRVEADKA TREGDLAQAS RILYGEIPAI QKELAAAEQA AEQEAEFAHQ DEPMVPDHVD
     ADSVAQIVSE WTGVPVGRLM QGENEKLLNM EDYLDKRVIG QGEAVQAVSD AVRRSRAGIS
     DPNRPTGSFL FMGPTGVGKT ELAKALADFL FDDEHAMVRI DMSEYMEKSS VSRLIGAAPG
     YVGYEEGGQL TEAVRRRPYS VVLFDEVEKA NPEVFDILLQ VLDDGRLTDG QGRTVDFKNT
     ILIMTSNLGS QFLINPDLSE QEKKDAVMNA VHAQFRPEFL NRLDETIIFQ PLTREELGKI
     VDLQVKQVAS RLTDRRITLD VTASAREWLA DTGYDPAYGA RPLRRLVQTE VGDQLARMLL
     AGQIKDGETV LVDHTGGEHL ELSVHEDDPM AGDTNPEDSE VKLSGSWPKV DPEEKEIGD
//
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