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Database: UniProt
Entry: A0A1G7BGE6_9FLAO
LinkDB: A0A1G7BGE6_9FLAO
Original site: A0A1G7BGE6_9FLAO 
ID   A0A1G7BGE6_9FLAO        Unreviewed;       866 AA.
AC   A0A1G7BGE6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN05421636_104116 {ECO:0000313|EMBL:SDE25295.1};
OS   Pricia antarctica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Pricia.
OX   NCBI_TaxID=641691 {ECO:0000313|EMBL:SDE25295.1, ECO:0000313|Proteomes:UP000199109};
RN   [1] {ECO:0000313|EMBL:SDE25295.1, ECO:0000313|Proteomes:UP000199109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23421 {ECO:0000313|EMBL:SDE25295.1,
RC   ECO:0000313|Proteomes:UP000199109};
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; FNAO01000004; SDE25295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7BGE6; -.
DR   STRING; 641691.SAMN05421636_104116; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199109; 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:SDE25295.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDE25295.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199109};
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..528
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   866 AA;  97488 MW;  2AD4E5667E5E82D3 CRC64;
     MNPNNYTIKS QEALQQAQQL AQSLGHQQIE NEHLFKAIWE VDENVLPFIL KKLNINVNLL
     QQILDKELQS FPKVSGGDIM LSREAGKTVN EASIIAKKME DEYISIEHLL LAILKSKSKI
     AHILKDQGAT EKDLKTAISE LRGGGKVTSQ SAEETYNSLE KYAQNLNRLA DTGKLDPVIG
     RDEEIRRILQ ILSRRTKNNP MLVGEPGTGK TAIAEGLAHR IVQGDVPENL KDKIIYSLDM
     GALIAGAKYK GEFEERLKSV IKEVTSSDGN IVLFIDEIHT LVGAGGGQGA MDAANILKPA
     LARGDLRAIG ATTLDEYQKY FEKDKALERR FQKVIVLEPD TESAISILRG IKEKYEAHHK
     VRIKDEAVIA AVELSQRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
     EIEIEAIKRE DDKAKLKSLN VDLANLKEDR NEIFAKWESE KSVVDNIQKT KQDIEEFKQE
     AERAERNGDY GKVAELRYGK IKEAQETLEI LQKELQEQQE GETLIKEEVT NEDIAEVVAK
     WTGIPVTKML QSEREKLLKL EDVLRNRVVG QEEAIEAVSD AIRRSRAGLQ DAKRPIGSFL
     FLGTTGVGKT ELAKTLAAYL FDDENALTRI DMSEYQERHS VSRLVGAPPG YVGYDEGGQL
     TEAVRRRPYS VVLLDEIEKA HPDTFNVLLQ VLDEGRLTDN KGRVADFKNT IIIMTSNMGS
     HIIQEKFENS KDIFSATEAA RVEVLDLLRK TIRPEFLNRI DDIIMFTPLS KKDITKIVKL
     QLDQLKKMIA KQHITIDATE EAIAYLAKKG YDPQYGARPI KRVIQKEVLN NLSKELLSGG
     ISAESIVLID SFDDGLVFRN QDELVE
//
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