ID A0A1E7Z293_9GAMM Unreviewed; 857 AA.
AC A0A1E7Z293;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RAP71221.1};
GN ORFNames=ACZ87_01966 {ECO:0000313|EMBL:RAP71221.1}, BBW68_07825
GN {ECO:0000313|EMBL:OFC62863.1};
OS Candidatus Erwinia dacicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=252393 {ECO:0000313|EMBL:OFC62863.1, ECO:0000313|Proteomes:UP000243534};
RN [1] {ECO:0000313|EMBL:OFC62863.1, ECO:0000313|Proteomes:UP000243534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL {ECO:0000313|EMBL:OFC62863.1,
RC ECO:0000313|Proteomes:UP000243534};
RA Yuval B.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAP71221.1, ECO:0000313|Proteomes:UP000244334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oroville {ECO:0000313|EMBL:RAP71221.1,
RC ECO:0000313|Proteomes:UP000244334};
RA Estes A.M., Hearn D.J., Agarwal S., Pierson E.A., Dunning-Hotopp J.C.;
RT "Genomes of the Obligate Erwinia dacicola and Facultative Enterobacter sp.
RT OLF Endosymbionts of the Olive Fruit fly, Bactrocera oleae.";
RL Submitted (APR-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:OFC62863.1}.
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DR EMBL; MAYS01000174; OFC62863.1; -; Genomic_DNA.
DR EMBL; LJAM02000181; RAP71221.1; -; Genomic_DNA.
DR RefSeq; WP_070134314.1; NZ_SEZT01000161.1.
DR AlphaFoldDB; A0A1E7Z293; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000243534; Unassembled WGS sequence.
DR Proteomes; UP000244334; 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:UP000244334};
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 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 857 AA; 95522 MW; 244FC1E5B81EA7B3 CRC64;
MHLDRLTNKF QLALADAQSL ALGHGNQFIE PLHLMSALFT QEGGSVRSLL TSASVDVSSL
RNAIEQALSR LPQVEGTYGD VQPSADLVRV LNLCDKLAQE RGDNFISSEL FVLAALDSRG
SLADLLKSAG ATSDKLTKAI DQMRRGDSVN DQGAEDQRQV LKKYTIDLTE RAELGKLDPV
IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLSL
DMGALIAGAK YRGEFEERLK AVLSDLSKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PSVEDTIAIL RGLKERYELH
HHVQITDPAI VAAATLVHRY IADRQLPDKA IDLIDEAASS IRMQIDSKPE SLDRLERRII
QLKLEQQALK KESDDASIKR LDMLEAELSQ KEHEYSALEE EWKAEKASLS GTQHIKTELE
NAKLAMEQAR RQGDLAQMSE LQYGKIPELE KQLESATQSE GKTMRLLRNR VTDVEIADVL
ARWTGIPVDR MMEGERDKML RMEQQLHTRV IGQNEAVEAV SNAIRRSRAG LADPNRPIGS
FLFLGPTGVG KTELCKALAN FMFDSDDAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEAGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
GSDLIQERFG ALSYDAMKEM VMAVVSQSFR PEFINRIDEL MVFHPLGEQH IASIARIQLT
RLYQRLEERG YELHISETAL QKLVENGYDP VYGARPLKRA IQHQIENPLA QQILSGALVP
GKIIQMDVEN DVIVAHQ
//