ID A0A087BET0_9BIFI Unreviewed; 904 AA.
AC A0A087BET0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BMAGN_1247 {ECO:0000313|EMBL:KFI69530.1};
OS Bifidobacterium magnum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1692 {ECO:0000313|EMBL:KFI69530.1, ECO:0000313|Proteomes:UP000029052};
RN [1] {ECO:0000313|EMBL:KFI69530.1, ECO:0000313|Proteomes:UP000029052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11591 {ECO:0000313|EMBL:KFI69530.1,
RC ECO:0000313|Proteomes:UP000029052};
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|ARBA:ARBA00004496,
CC 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:KFI69530.1}.
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DR EMBL; JGZB01000001; KFI69530.1; -; Genomic_DNA.
DR RefSeq; WP_051126635.1; NZ_JGZB01000001.1.
DR AlphaFoldDB; A0A087BET0; -.
DR STRING; 1692.BMAGN_1247; -.
DR eggNOG; COG0542; Bacteria.
DR Proteomes; UP000029052; 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 78, MITOCHONDRIAL; 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:UP000029052};
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 870..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 904 AA; 99131 MW; AB3FEC07C0F1ACC3 CRC64;
MEQKYTTLAQ EALSDAIQSA AAAGNPQVDT LHLLDVLMRQ ENSIVVPLIE AAGGSRQIIG
AAVRRALTDL PSATGSSTSQ PQASRQLSAV LSQAADDMKT MGDDYISCEL LLLAIAQAMP
NRAGEILQQN GVTPEAIDKA IPELRGGAKV TSPDAEGSYK ALEKYSTDLT ERAREGKLDP
VIGRDQEIRR VIQILSRRTK NNPVLIGEPG VGKTAVVEGL ALRIVAGDVP STLQNKKLIS
LDLGSMVAGS KYRGEFEERL KSVLDEIKQS DGQIITFIDE LHTVVGAGSA EGSMDAGNML
KPMLARGELR LIGATTLDEY RENIEKDPAL ERRFQQVFVG EPSVEDTIAI LRGLKERYEA
HHKVTIGDDA LVAAATLSNR YITGRQLPDK AIDLVDEAAA HLRMELDSQP EEIDELQRKV
TRLEMEEMQL SKETDDPASQ DRLKKLREDL ANTKEHLNGL KARWDAEKAG HNKVGDLRAR
LDSLRVQADK ATRDGDLAKA SKILYGDIPA IQKQLADAEH EAEQEADLAH KEEPMVPDHV
DADSVAGIVA EWTGIPVGRL MQGENEKLLN MEEYLGKRVI GQSEAVQAVS DAVRRSRAGL
SDPNRPTGSF LFLGPTGVGK TELAKALADF LFDDERAMVR IDMSEYMEKS SVSRLIGAAP
GYVGYEEGGQ LTEAVRRRPY SVVLFDEVEK ANSEVFDILL QVLDDGRLTD GQGRTVDFKN
TILIMTSNLG SQFLVNPDLD EKAKEKAVMD TVHAQFRPEF LNRLDDVVMF QPLSRKELGR
IVDLQVKQVA SRLTDRRITL DVTEAAREWL ANTGYDPAYG ARPLRRLVQT EVGDAMAKML
LGGKIHDGKT VLVDHTGGDH LEFKVYDVDP ELGDTNPDDS QLEINGADDG WKAAESTDDE
DEAR
//
