ID C0BZT1_9FIRM Unreviewed; 887 AA.
AC C0BZT1;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:EEG74659.1};
GN ORFNames=CLOHYLEM_05323 {ECO:0000313|EMBL:EEG74659.1};
OS [Clostridium] hylemonae DSM 15053.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=553973 {ECO:0000313|EMBL:EEG74659.1, ECO:0000313|Proteomes:UP000004893};
RN [1] {ECO:0000313|EMBL:EEG74659.1, ECO:0000313|Proteomes:UP000004893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG74659.1,
RC ECO:0000313|Proteomes:UP000004893};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium hylemonae (DSM 15053).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG74659.1, ECO:0000313|Proteomes:UP000004893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15053 {ECO:0000313|EMBL:EEG74659.1,
RC ECO:0000313|Proteomes:UP000004893};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2009) 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:EEG74659.1}.
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DR EMBL; ABYI02000019; EEG74659.1; -; Genomic_DNA.
DR AlphaFoldDB; C0BZT1; -.
DR STRING; 553973.CLOHYLEM_05323; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR Proteomes; UP000004893; 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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 26..168
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 427..548
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 887 AA; 99714 MW; F9C47C819A1C9E59 CRC64;
MLTIFVIVRI EQIKNYAGEE VVTMNINKFT QKSLQAVQDC ERTAMEYGNQ EIEQEHLLYA
LLVQDDSLIL KLMEKMGVEK TVFINRVEEG LRKRTKVQGG QAFVGQDLNK ALIHAEDEAK
QMGDEYVSVE HLFLSLLKYP NKELKVIFRE LGIKRDLFLQ ALATVRGSQK VTSDNPEATY
DTLNKYGSDL VERARDQKLD PVIGRDSEIR NLVRILSRKT KNNPVLIGEP GVGKTAVVEG
LAQRIVRGDV PEALKDKTIF SLDMGALVAG AKYRGEFEER LKAVLEEVKN SDGKIILFID
ELHTIVGAGK TDGAMDAGNM LKPMLARGEL HCIGATTLDE YRQYIEKDAA LERRFQPVLV
DEPTVEDAIS ILRGLKERYE VFHGVKITDG ALVAAATLSD RYISDRFLPD KAIDLVDEAC
ALIKTELDSM PAELDELQRK IMQLEIEEAA LKKEEDRLSK DRLGHLQQEL AELREQFAGK
KAQWDNEKVK VERVQKVREE IEQVNKEIQK AQQSYDLEKA AELQYGRLPQ LKKQLEEEEG
KIKDEERSLV HESVTDEEIA RIVSRWTGIP VARLNESERS KTLHLADELH RRVIGQEEGV
ELVTEAIIRS KAGIKDPGKP IGSFLFLGPT GVGKTELAKA LAESLFDDEN NMVRIDMSEY
MEKYSVSRLI GAPPGYVGYD EGGQLTEAVR RKPYSVVLFD EVEKAHPDVF NVLLQVLDDG
RITDSQGRTV DFKNTILIMT SNIGSAYLLD GIDEAGNISQ ESQNAVMDDL RAHFRPEFLN
RLDEMIMFKP LTKENIYAII DLLTEDVNKR LADKEISISL TEAAKNMVVE GGYDPTYGAR
PLKRYLQKNV ETLAAKLMLQ GDIGAGETIV IDVENGKLAA GARKNLL
//