ID A0A1I7IK36_9CLOT Unreviewed; 865 AA.
AC A0A1I7IK36;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04487886_11232 {ECO:0000313|EMBL:SFU73248.1};
OS Clostridium sp. DSM 8431.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1761781 {ECO:0000313|EMBL:SFU73248.1, ECO:0000313|Proteomes:UP000198524};
RN [1] {ECO:0000313|EMBL:SFU73248.1, ECO:0000313|Proteomes:UP000198524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8431 {ECO:0000313|EMBL:SFU73248.1,
RC ECO:0000313|Proteomes:UP000198524};
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; FPBY01000123; SFU73248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7IK36; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198524; 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:SFU73248.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFU73248.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198524};
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..497
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 97661 MW; 51E63D9E89F53EA4 CRC64;
MDIDKMTLRV QKALSDANVI AVRNDHQQIE TIHVFAALME QEDGLIPNIL NKMGISTKEV
TAKINSKLSS MPKVLGEGAN SSGVYITRQV ESVLVKAEEI SKQFKDSFVS VEHLMLALMD
VDSNGPVGEI LKSFNINKKD FMQVLEQVRG NQKVDTQDPE GTYDALAKYG TNLVELAKKH
KLDPVIGRDE EIRRAIRILS RRTKNNPVLI GEPGVGKTAI VEGLAERIVR GDVPEGLKDR
IIFSLDMGSL IAGAKYRGEF EERLKAVLKE VQSSEGKIIL FIDEIHTIVG AGKTDGAMDA
GNLIKPLLAR GELHCIGATT FDEYRQYIEK DKALERRFQP VIVNEPTVED TISILRGLKE
KFEIHHGIRI HDSAIVAAAK LSDRYVQDRY LPDKAIDLID EAGSMVRSEI DSLPTELDVL
RRKKFQLETE KEALEKENDE GSKKRLAALN KELADIKEKD DEMTAKYEKE KEHIMALRDL
KTQLDDARGE VEKYQRQYDY NKVAELQYST IPRLEEAIAK KEAEVKENYD GALLKEEVTE
EEISEVLSKW TGIPVNNLLE GEREKLLRLD EELQRRVIGQ DRAVEAVSSA ILRARAGLKD
ENKPIGSFLF LGPTGVGKTE LAKTLARTLF DTEDAMIRID MSEYMEKHAV SRLVGAPPGY
VGYEQGGQLT EAVRRRPYSV LLFDEIEKAH PDVFNMFLQI LDDGRLTDNK GKTVDFKNTI
IIMTSNIGSQ YLLDNEGEEV SDENRELVMQ ALRSKFKPEF LNRVDDTIMF KPLSEDGIKK
IIEIFLDEVR ERLKDRNITL EITDKAKSIL AREGYDPVYG ARPLKRYIQN TLENSLARKI
IKGEVHYGST VVVDATEDEL TLSTR
//