ID A0A1G5AD81_9FIRM Unreviewed; 860 AA.
AC A0A1G5AD81;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN02910433_00090 {ECO:0000313|EMBL:SCX75797.1};
OS Blautia sp. SF-50.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1520805 {ECO:0000313|EMBL:SCX75797.1, ECO:0000313|Proteomes:UP000198516};
RN [1] {ECO:0000313|Proteomes:UP000198516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-50 {ECO:0000313|Proteomes:UP000198516};
RA Varghese N., Submissions S.;
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; FMUW01000001; SCX75797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5AD81; -.
DR Proteomes; UP000198516; 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:SCX75797.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SCX75797.1};
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..525
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 860 AA; 96967 MW; 092A954A0A75D9F1 CRC64;
MNISKFTQKS VQAVQDLEKI AYEYGNQEIE EEHLLYALLT QEDSLILKLI EKMEIQKEYF
IDTVKRALDA RVKVSGGELR FGQYLNKALV SAEDEAKAMG DEYVSVEHLF LSMLKNPSPS
MKKLFNEFGI TRERFLQALS TVRGNQRVVS DNPEATYDTL NKYGEDLVEK AKNQKLDPVI
GRDMEIRNII RILSRKTKNN PVLIGEPGVG KTAAIEGLAQ RIVAGDVPEG LKNKKIFALD
MGALVAGAKY RGEFEERLKA VLEEVKKSEG QIILFIDELH LIVGAGKTDG AMDAGNMLKP
MLARGELHCI GATTLDEYRQ YIEKDAALAR RFQPVMVNEP TVEDTISILR GLKERYEVFH
GVKITDSALV AAATLSHRYI TDRFLPDKAI DLVDEACALI KTELDSMPTE LDEQRRKIMQ
LEIEESALKK ETDNLSKERL ADLQKELAEL RDTFNTQKAQ WDNEKHSVEK LQKLREQIED
INKQIQKAKQ NYDLEKAAEL QYGELPKLQQ QLEIEEKQVK ESDRSLVHEA VTDDEIARII
SRWTGIPVTK LTEGERTKLL GLEDELHKRV VGQDEGVRLV TDAILRSKAG IKDPTKPIGS
FLFLGPTGVG KTELAKTLAA TLFDDEQNMV RIDMSEYMEK YSVSRLIGAP PGYVGYEEGG
QLTEAVRRKP YSVVLFDEIE KAHPDVFNVL LQVLDDGRIT DSQGRTVDFK NTILIMTSNI
GSPYLLDGID EKGDIKPEAQ EQVMNDLRGH FRPEFLNRLD EIIMFKPLTK DNVGKIVDLM
VKELSDRLAD QELSLELTDA AKQMVVDNGY DPVYGARPLK RYLQNYVETL TAKKILSGDV
HAGDTIVLDV KDGAFTVSTK
//