ID A0A1H3XNE0_9FIRM Unreviewed; 868 AA.
AC A0A1H3XNE0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04515656_102139 {ECO:0000313|EMBL:SEA00957.1};
OS Eubacterium aggregans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=81409 {ECO:0000313|EMBL:SEA00957.1, ECO:0000313|Proteomes:UP000199394};
RN [1] {ECO:0000313|EMBL:SEA00957.1, ECO:0000313|Proteomes:UP000199394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR12 {ECO:0000313|EMBL:SEA00957.1,
RC ECO:0000313|Proteomes:UP000199394};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNRK01000002; SEA00957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3XNE0; -.
DR STRING; 81409.SAMN04515656_102139; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199394; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:SEA00957.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEA00957.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199394};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 417..531
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 97400 MW; D52FA67056DC8F9C CRC64;
MDMNMLTQKS IEAVKDAEKI ALDHNAPEIE PDHLLLALVT QENGVVSRIF ERMGKATYPI
IEELKRLVAN KPSISGPGRE PGKVYISRDT EKVLNEAYKI AKNMDDQYIS VEHILLGMFD
LGKKSPVVEL LGRYGITKAS IDTVLNDVRG GQKVTSDHPE TTYEALAQYG HDLVQDCMDN
KLDPVIGRDS EIRHTIRILS RKTKNNPVLI GEPGVGKTAI VEGLAARIVA GDVPEGLKGK
RIISLDLGAL VAGAKYRGEF EERFKAVLKE VKDSDGEIIL FIDELHTIVG AGKTDGAMDA
GNMLKPMLAR GELHCIGATT LDEYRQYIEK DPALERRFQP VMVDEPTVED TIAILRGLKE
RYEIFHGVKI LDNALVSAAV LSNRYISDRF LPDKAIDLVD EACAMIRTEI DSMPVEMDEV
NRKIIQMEIE EAALKKDDDK LSKERLERLQ KELAEYKDDF NGMKIQWQNE KDAVEEVQKV
KEEIDSVNHQ IEKAEREYDL DKAAELKYGK LPELKKKMEE LEALAESKGA DESLIRERVS
EEEIAEIISN WTGIPLSKLV SGEREKLLNL EETLEERVIG QEEPIKKVVD AIIRSRAGIK
NPNTPIGSFL FLGPTGVGKT ELAKAVAANL FDTENNMVRI DMSEYMEKFS VSRLIGAPPG
YVGYEEGGQL TEAVRRKPYS VILLDEIEKA HKDVFNILLQ VLDDGRITDS QGRTVDFKNT
IIIMTSNIGS EFLLEGIGPD GEIKEETEDA VMSSLRNYFR PEFLNRIDEI VLYKPLSRES
ITHIVDLMMA ELQKRLEDNR LSVVLTEGAK EAIIDQGYDP SYGARPLKRF IQKNIETMVG
KEIIRGSLDE GDVLTIDFKD GRFTVIAD
//