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Database: UniProt
Entry: A0A1H2FJE2_9FLAO
LinkDB: A0A1H2FJE2_9FLAO
Original site: A0A1H2FJE2_9FLAO 
ID   A0A1H2FJE2_9FLAO        Unreviewed;       868 AA.
AC   A0A1H2FJE2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN04487762_1654 {ECO:0000313|EMBL:SDU07486.1};
OS   Polaribacter sp. Hel1_33_78.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1336804 {ECO:0000313|EMBL:SDU07486.1, ECO:0000313|Proteomes:UP000198843};
RN   [1] {ECO:0000313|EMBL:SDU07486.1, ECO:0000313|Proteomes:UP000198843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hel1_33_78 {ECO:0000313|EMBL:SDU07486.1,
RC   ECO:0000313|Proteomes:UP000198843};
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; LT629794; SDU07486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2FJE2; -.
DR   STRING; 1336804.SAMN04487762_1654; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000198843; Chromosome i.
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:SDU07486.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDU07486.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198843};
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   868 AA;  97761 MW;  92467EEA53600FDE CRC64;
     MNLNNYTTKS QETIQMAQQI AQSFSHNQIE NEHFFKALTQ VDKNVLPFLL KKLNINSIVV
     DQILDKQLES LPKVSGAELM ISREAGKTLT EAAVIAKKMK DDYVSIEHLI LAIFKSKSNI
     AQVLKDQGVT EKHLLAAIEE LRKGERVTSQ SQEETYNSLN KYAKNLNKLA EDGKLDPVIG
     RDEEIRRLLQ ILSRRTKNNP ILVGEPGTGK TAIAEGLAHR IVDGDVPENL KDKLIFSLDM
     GALIAGAKYK GEFEERLKAV INEVTISAGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
     LARGELRAIG ATTLDEYQKH FEKDKALERR FQKIIVNEPD TESAISILRG IKEKYETHHK
     VRIKDEAIIG AVELSQRYIS NRFLPDKAID LMDEAMAKLR MEINSKPEEL DVLDRKVMQL
     EIEIEAIKRE KDEVKLKSLR SDLANLKEER NEMSAKWKSE KEVVDNIQNA KLVIENFKIE
     AEKAERDGDY GKVAEIRYGK IKTAQENLEQ LQKDLQENQS ESSLIKEEVT YEDIAEVVAK
     WTGVPVTKMI QSEREKLLKL EDQLHKRVVG QEEAIIAVSD AVRRSRAGLQ NPSKPIGSFL
     FLGTTGVGKT ELAKALASYL FDDENAMTRI DMSEYQERHS VSRLIGAPPG YVGFDEGGQL
     TEAVRRRPYS VVLLDEIEKA HPDTFNVLLQ VLDEGRLTDN KGRVADFKNT IIIMTSNMGS
     HIIQEKFSDP KADLESITEL AKVEVLGLLK QSVRPEFLNR IDDIIMFTPL TKSDIFEIVK
     LQLAHLKKMI GKQDIYIDAT DEAIEYLARK GYQPEFGARP VKRVIQKEVL NQLSKDILSG
     KVTTDSIILL DAFDDQLVFR NQSDLVQN
//
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