ID A0A3N2NR47_9BACT Unreviewed; 865 AA.
AC A0A3N2NR47;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:ROT24136.1};
GN ORFNames=EEL53_02200 {ECO:0000313|EMBL:ROT24136.1};
OS Muribaculaceae bacterium Isolate-114 (HZI).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486475 {ECO:0000313|EMBL:ROT24136.1, ECO:0000313|Proteomes:UP000273368};
RN [1] {ECO:0000313|EMBL:ROT24136.1, ECO:0000313|Proteomes:UP000273368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-114 (HZI) {ECO:0000313|Proteomes:UP000273368};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-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:ROT24136.1}.
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DR EMBL; RIBN01000002; ROT24136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2NR47; -.
DR Proteomes; UP000273368; 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 Reference proteome {ECO:0000313|Proteomes:UP000273368};
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 403..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 97758 MW; 7C17A530F4F4E5EC CRC64;
MNFNNFTIKS QEVVQKAIDF TKQSGQQQIE PVHLLKAIIS ESETIVNFIF QKLGANLNGV
KMGVDQTIAS LPRVSGGDVM LSRESNEALQ KSVDFSKSMG DEYVSVEAIM MGILKTGCKA
SQILKDNGIT EDGLKAAISE LRKGNTVKDQ SAEESYQSLS KYAINLNDRA RNGKLDPVIG
RDEEIRRVLQ ILSRRTKNNP MLVGEPGTGK TAIAEGLAMR IVRGDVPENL KSKQIYSLDM
GALVAGAKYK GEFEERLKAI VNEVTQSDGE IILFIDEIHT LVGAGKGEGA MDAANILKPA
LARGELRSIG ATTLDEYQKY FEKDKALERR FQKVMVDEPD EMSAISILRG LKERYENHHK
VRIMDEAIIA AVQLSVRYIT DRFLPDKAID LIDEAASKLR LEMDSQPQAL DEASRKIKQL
EIEREAIKRE KDSYKLKEID EELANLRDTE KSLRAKWKAE KNEINKIQQN KIDIEQLNYE
ADRAEREGDY AKVAEIRYSK IKQKEDENKE IQLKLKELQG EGAMIKEEVD AEDIAEVVSR
WTGIPVKKMA QSEKEKLLHL EEELHHRVVG QEDAIRAVSD AVRRSRAGLN DPRRPIGSFI
FLGTTGVGKT ELAKALAEYL FDDEDMMTRI DMSEYMEKHS VSRLVGAPPG YVGYEEGGQL
TEAVRRKPYS VVLFDEIEKA NPDVFNILLQ VLDDGRLTDN KGRFINFKNT IIIMTSNMGS
DIIRQNFQGF SDKNEEKKQE IIASTKQDVM DRLKQIIRPE FLNRIDETVM FTPLDKKEIL
EIVELQVKSV KKMLTTNGIT LDVTKDALDL LAEDGYDPEF GARPVKRTIQ RMVLNQLSKD
ILAQKVDRDH PIVIDRQGDT LVFKN
//