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Database: UniProt
Entry: J3VRB0_9ENTR
LinkDB: J3VRB0_9ENTR
Original site: J3VRB0_9ENTR 
ID   J3VRB0_9ENTR            Unreviewed;       857 AA.
AC   J3VRB0;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   13-SEP-2023, entry version 58.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=A359_00770 {ECO:0000313|EMBL:AFP84481.1};
OS   secondary endosymbiont of Ctenarytaina eucalypti.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts.
OX   NCBI_TaxID=1199245 {ECO:0000313|EMBL:AFP84481.1, ECO:0000313|Proteomes:UP000003936};
RN   [1] {ECO:0000313|EMBL:AFP84481.1, ECO:0000313|Proteomes:UP000003936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ceuc_S {ECO:0000313|EMBL:AFP84481.1};
RX   PubMed=22821013; DOI=10.1093/molbev/mss180;
RA   Sloan D.B., Moran N.A.;
RT   "Genome reduction and co-evolution between the primary and secondary
RT   bacterial symbionts of psyllids.";
RL   Mol. Biol. Evol. 29:3781-3792(2012).
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:RU362034}.
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DR   EMBL; CP003546; AFP84481.1; -; Genomic_DNA.
DR   RefSeq; WP_014887779.1; NC_018419.1.
DR   AlphaFoldDB; J3VRB0; -.
DR   STRING; 1199245.A359_00770; -.
DR   KEGG; sect:A359_00770; -.
DR   PATRIC; fig|1199245.3.peg.94; -.
DR   HOGENOM; CLU_005070_4_1_6; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000003936; Chromosome.
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; 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; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362034};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU362034};
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:RU362034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003936};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          405..461
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   857 AA;  96352 MW;  7B27AE809296F978 CRC64;
     MPLERLTNKF QLALAESQSI ARRRGNQVIE PLHVIAALLK KESYIWQPLL EAAGVNVLAF
     ISAVEHACDR LPQCKVTGVD IQPSQALLHL LNQCDKLAKK RAEPFISSEL FLLALLKSRG
     TLAELLKSAG TTSAVIDRAI ENVLAGEQGN EQGLEDRRLA LKKFTVDLTA RAAQGKLDPV
     IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKKNRVLSL
     DMGSLVAGAK YRGEFEERLK SVLNDLLKEE GNVTLFIDEL HTMIGAGNAE GTIDACNMLK
     PALARGELHC IGATTLDEYR KFIEKDAALE RRFQKVFVVE PNVENTIAIL RGLKERYELH
     HNVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS IRIQIDSKPE ELDRLERRIM
     QLKLEQQALK KESDEASIKR LALLHDELAK KESDYSALEE KWKAEKASLS GTQYLKATLE
     QAKISIEQAR RACDLARMSE LQYGTIPELE KKLEAAATFK EEGFCLLRNR VTDIEIAEVV
     ARWTGIPVSR MLESEREKLL RMEQDLHQWV IGQHEAVEAV SNAIRRSRAG LADPNRPIGS
     FMFLGPTGVG KTELCKALTT FLFDSYDAML RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
     YLTETVRRRP YSVILLDEIE KAHPDVFNIL LQVLDDGRLT DSQGRTVDFR NTVVIMTSNL
     GSELIQERFG QMSYQEMKRI VLDVVSHHFR PEFLNRVDEI VVFHPLSRED ISDIVQIQLQ
     RLYQRLEERG YKTTISEEVL ALLEQSGFDP VYGARPLKRT IQQAIENPLS QQILSGQLLP
     GKPVHLQVLD EHIVARQ
//
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