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
//