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
//