ID A0A416JWW1_9FIRM Unreviewed; 863 AA.
AC A0A416JWW1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RHQ17947.1};
GN ORFNames=DW974_04945 {ECO:0000313|EMBL:RHQ17947.1};
OS Lachnospiraceae bacterium AM48-27BH.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=2292271 {ECO:0000313|EMBL:RHQ17947.1, ECO:0000313|Proteomes:UP000285913};
RN [1] {ECO:0000313|EMBL:RHQ17947.1, ECO:0000313|Proteomes:UP000285913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM48-27BH {ECO:0000313|EMBL:RHQ17947.1,
RC ECO:0000313|Proteomes:UP000285913};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RHQ17947.1}.
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DR EMBL; QUFC01000006; RHQ17947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A416JWW1; -.
DR Proteomes; UP000285913; 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:UP000285913};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 405..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 97235 MW; 747EB158801E6972 CRC64;
MNINKFTQKS MEAVQNCEKL AYEHGNQQLE QEHLLYSLLT LEDSLILKLI TKMNISKEMF
MNEAEQAVNR LTKVSGGGQL YVSNDLNKVL ISAEDEAKAM GDEYVSVEHL FLAMLKQPDK
TLKELFKQYG ITRESFLQAL STVRGNQRVV SDNPEATYDT LEKYGYDLVE RARNQKLDPV
IGRDSEIRNV VRILSRKTKN NPVLIGEPGV GKTAVVEGLA QRIVRGDVPE GLKDKKLFAL
DMGSLVAGAK YRGEFEERLK AVLEEVKKSE GQIILFIDEL HTIVGAGKTE GSMDAGNMLK
PMLARGELHC IGATTLDEYR KYIEKDPALE RRFQPVTVDE PTVEDTISIL RGLKERYEVY
HGVKITDSAL VAAATLSDRY ISDRFLPDKA IDLVDEACAM IKTELDSMPA ELDELSRKIM
QMEIEEAALK KETDHLSQDR LAELQKELAE LHDQFATKKA QWENEKSSVD KLSSLREEIE
AVNREIAQAQ QKYDLNKAAE LQYGKLPELQ KQLEAEEEKV KNQDLSLVHE SVTEDEIARI
VSKWTGIPVA KLNESERSKT LHLDEILHKR VVGQDEGVEK VTEAIIRSKA GIKDPSKPIG
SFLFLGPTGV GKTELAKALA ECLFDDESNM VRIDMSEYME KHSVARLIGA PPGYVGYEEG
GQLTEAVRRK PYCVVLFDEV EKAHPDVFNV LLQVLDDGRI TDSTGKTVDF KNTIIIMTSN
IGSQYLLDGI DEKGNIKEDA QQLVMNDLRG HFRPEFLNRL DEIIMFKPLT KDNITHIVDL
MIADTNKRLE DREIKVELTD EAKKYVVDHG YDPVYGARPL KRYLQKNVET LAAKVILGDQ
LRAGNTIVID TSEDGQKLIA HIE
//
