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Database: UniProt
Entry: A0A087CM99_9BIFI
LinkDB: A0A087CM99_9BIFI
Original site: A0A087CM99_9BIFI 
ID   A0A087CM99_9BIFI        Unreviewed;       889 AA.
AC   A0A087CM99;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BREU_1168 {ECO:0000313|EMBL:KFI84399.1};
OS   Bifidobacterium reuteri DSM 23975.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI84399.1, ECO:0000313|Proteomes:UP000028984};
RN   [1] {ECO:0000313|EMBL:KFI84399.1, ECO:0000313|Proteomes:UP000028984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI84399.1,
RC   ECO:0000313|Proteomes:UP000028984};
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:KFI84399.1}.
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DR   EMBL; JGZK01000017; KFI84399.1; -; Genomic_DNA.
DR   RefSeq; WP_044089866.1; NZ_JGZK01000017.1.
DR   AlphaFoldDB; A0A087CM99; -.
DR   STRING; 1437610.BREU_1168; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000028984; 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:UP000028984};
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          516..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          84..111
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          406..493
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   889 AA;  96541 MW;  033B8C58E3423303 CRC64;
     MEQKFTTMAQ EAVGDAIQSA SAAGNAQVET LHVMDALLRQ ENGVVRSLIE AAGGNAQAIG
     AAVRNALVAL PSASGSTTSQ PQASRQLTAA IAQAEKEMQQ MGDEYVSTEH LLIGIAASKP
     NQSAEILEKN GVTAAALRKA VPGVRGGAKV TSPDAEGSYK ALEKYSTDLT ARAKEGKLDP
     VIGRDQEIRR VIQILSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVAGDVP TTLQGKKLIS
     LDLGSMVAGS KYRGEFEERL KAVLNEIKNA NGQIVTFIDE IHTIVGAGAA EGSMDAGNML
     KPMLARGELR LIGATTLDEY RENIEKDPAL ERRFQQVYVG EPSVEDTIAI LRGLKQRYEA
     HHKVTIGDDA LVAAATLSNR YISGRQLPDK AIDLVDEAAA HLRMELDSSP EEIDELQRKV
     TRLEMEEMQL KKAEDPASKE RLGKLQAELA DTREKLSGLK ARWDAEQAGH NKVGELRAKL
     DDLRVQADKF TREGNLAEAS KILYGEIPAI QKELAAAENA DAESKDTGST DPNSEPMVPD
     RVDADSVAEI VSDWTGIPVG RLMQGENEKL LHMEDYLGKR VIGQKEAIQA VSDAVRRSRA
     GISDPNRPTG SFLFLGPTGV GKTELAKALA DFLFDDEKAM VRIDMSEYME KASVSRLIGA
     APGYVGYEQG GQLTEAVRRR PYSVVLFDEV EKANPEIFDV LLQVLDDGRL TDGQGRTVDF
     KNTILIMTSN LGSQFLVNED LDADAKKKAV MDAVHMNFKP EFLNRLDDIV MFHPLTREEL
     GGIVDIQVNA VAQRLTDRRI TLDVTDSARE WLANTGYDPA YGARPLRRLV QTEVGDQLAR
     MLLAGKVHDG DTVLVDHTGG EHLELSAWAS DQIVGDDPDV EVGNVSEDK
//
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