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Database: UniProt
Entry: A0A1H3XNE0_9FIRM
LinkDB: A0A1H3XNE0_9FIRM
Original site: A0A1H3XNE0_9FIRM 
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
//
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