ID A0A5C7EPN2_9ACTN Unreviewed; 867 AA.
AC A0A5C7EPN2;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TXF36982.1};
GN ORFNames=E4J93_03800 {ECO:0000313|EMBL:TXF36982.1};
OS Collinsella sp. BA40.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=2560852 {ECO:0000313|EMBL:TXF36982.1, ECO:0000313|Proteomes:UP000321063};
RN [1] {ECO:0000313|EMBL:TXF36982.1, ECO:0000313|Proteomes:UP000321063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA40 {ECO:0000313|EMBL:TXF36982.1,
RC ECO:0000313|Proteomes:UP000321063};
RA Park J.-K.;
RT "Collinsella canisensis sp. nov., a novel bacterium isolated from canine
RT feces.";
RL Submitted (AUG-2019) 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:RU362034}.
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:TXF36982.1}.
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DR EMBL; VOWY01000009; TXF36982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C7EPN2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000321063; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362034};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU362034};
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:RU362034};
KW Reference proteome {ECO:0000313|Proteomes:UP000321063};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 411..532
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 95651 MW; 7B5198B4BFBF2125 CRC64;
MRIDKLAMTS KEALQNAIAI AGDASAGSVE PVHLLASLLT GGERNISVII ERIGADPKRL
ALVTQQAIEA APQVSGGAQI GLSGELTRVL DRAEKFASKM EDNFVVTEHL LMALAEDRGQ
AGRILADAGV TRERIEEVYT ELRGDDRVTS EDDRLQFEAL EQYGRNVCDL ARAGKLDPVI
GRTEEIRRTI QVLSRRTKNN PVLIGEPGVG KTAIVEGIAQ RIVAGDVPST LRDRDIIELD
MSALVAGAKY RGEFEDRLKA VLKEVERANG RVILFIDELH TIVGAGATEG SMDAGNILKP
ALARGDLHAI GATTLDEYRK YIEKDAALAR RFQQVMVSEP SVEDTISILR GLKEKYEIFH
GVHITDGALV AAADLSSRYI ADRFLPDKAI DLVDEAASRL RMELDSMPVE IDAITRQLTQ
MQIEEQALMK ETDDASRERL EALRQEIATA QEQLNVAKAG WLNQKNAIDR IQELKGRIDD
AKGELERATR DGNFERAGEL RYSVIPSLEA DRAQAEEALD AQKESGEGLK EQVTSDEIAE
VVSAWTGVPV AKMMQGELDK LKTLEDELHR RVIGQDEAVR AVAAAVRRSR AGLADPDRPI
GSFFFLGPTG VGKTELAKAL AECLFDDERA LVRIDMSEYM EKFSVQRLIG APPGYVGYDE
GGQLTEAVRR RPYSVILLDE MEKAHPDVFN VLLQVLDDGR LTDGQGRQVS FKNTIIIMTS
NVGSSAIAEY AGHDEQEMRR QVDEAMSHTF RPEFLNRIDD IVVFHPLGME QIERIVDIQL
ADVRRRMAKE RMTLAITPAA KQMLAVGGLD PVFGARPLKR LIQREVVDAI ARAIIDGRVR
EGDEVTVDVD AQNNFVVSDV ESVRYEA
//