ID A0A420DLG0_9FLAO Unreviewed; 868 AA.
AC A0A420DLG0;
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 ORFNames=BXY80_1298 {ECO:0000313|EMBL:RKE95114.1};
OS Ichthyenterobacterium magnum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ichthyenterobacterium.
OX NCBI_TaxID=1230530 {ECO:0000313|EMBL:RKE95114.1, ECO:0000313|Proteomes:UP000284892};
RN [1] {ECO:0000313|EMBL:RKE95114.1, ECO:0000313|Proteomes:UP000284892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26283 {ECO:0000313|EMBL:RKE95114.1,
RC ECO:0000313|Proteomes:UP000284892};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (SEP-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:RKE95114.1}.
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DR EMBL; RAQJ01000002; RKE95114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420DLG0; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000284892; 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 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 Hydrolase {ECO:0000313|EMBL:RKE95114.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RKE95114.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000284892};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..521
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 97306 MW; 8D33FA0AEF7F1DBE CRC64;
MNFNNYTIKS QEAIQQAQQL AQSYGHQQIE NEHLFKGILE VDENVLPFLL KKLNVNTSLL
EQILDKELES FPKVSGTDIM LSREAGKSLN EASIIAKKMN DDFVSIEHLL LAIFKSKSKI
AQILKDQGVT EKALKASIDE LRKGDRVTSQ SQEDTYNSLN KYAKNLNQLA KDGKLDPVIG
RDEEIRRILQ ILSRRTKNNP ILVGEPGTGK TAIAEGLAHR IIDGDIPENL VDKQIFALDM
GALIAGAKFK GEFEERLKAV IKEVTTSEGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVMVDEPD TESAISILRG IKEKYETHHK
VRIKDEAIIG AVELSSRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
EIEIEAIKRE KDESKLKSLR SDLANLKEER NEINAKWKSE KEVVDNIQIA KQDIENYKLE
AERAEREGDY GKVAELRYGK IKEATEALEG FQKQLAAQQE NALIKEEVTY EDIADVVAKW
TGIPVTKMIQ SEREKLLKLE DELHKRVVGQ DEAIVAVSDA VRRSRAGLQN PQKPIGTFLF
LGTTGVGKTE LAKALAEYLF DDENAMTRID MSEYQERHSV SRLVGAPPGY VGYDEGGQLT
EAVRRKPYSV VLLDEIEKAH PDTFNILLQV LDEGRLTDNK GRIADFKNTI IIMTSNMGSH
IIQERVEAIK DINAAMDSAK VDVLGLLKQS VRPEFLNRID DTIMFTPLSK DNIAAIVGLQ
LKGITKMIAQ QGITFDATEE AIAYLAEKGY EPEYGARPVK RVIQKEVLNA LSKEILAGKV
TTDSIILLDA FDDELVFRNQ GNLVTEEF
//
