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Database: UniProt
Entry: A0A3N2NR47_9BACT
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Original site: A0A3N2NR47_9BACT 
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
//
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