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Database: UniProt
Entry: D3CZ50_9ACTN
LinkDB: D3CZ50_9ACTN
Original site: D3CZ50_9ACTN 
ID   D3CZ50_9ACTN            Unreviewed;       870 AA.
AC   D3CZ50;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=FrEUN1fDRAFT_2821 {ECO:0000313|EMBL:EFC84094.1};
OS   Parafrankia sp. EUN1f.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Parafrankia.
OX   NCBI_TaxID=102897 {ECO:0000313|EMBL:EFC84094.1, ECO:0000313|Proteomes:UP000004777};
RN   [1] {ECO:0000313|EMBL:EFC84094.1, ECO:0000313|Proteomes:UP000004777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EUN1f {ECO:0000313|EMBL:EFC84094.1,
RC   ECO:0000313|Proteomes:UP000004777};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Larimer F., Land M.L., Hauser L., Beauchemin N., Sen A.,
RA   Fernandez M., Tisa L.;
RT   "The draft genome of Frankia sp. EUN1f.";
RL   Submitted (JAN-2010) 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:EFC84094.1}.
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DR   EMBL; ADGX01000037; EFC84094.1; -; Genomic_DNA.
DR   RefSeq; WP_006540664.1; NZ_ADGX01000037.1.
DR   AlphaFoldDB; D3CZ50; -.
DR   Proteomes; UP000004777; 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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          85..112
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          414..501
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   870 AA;  94752 MW;  F3B32A1239A15D7E CRC64;
     MNADRLTARS QEALSSAISR ATGDGSPLVD PLHLLTALLE AHDGVGAALL DAVGVDAAAV
     RSRAEAAVGR LPRAAGANVA PPQLSRQLVA VLNNAERQAA RMSDEYISVE HLVVALAEEG
     GEASRILADT GATADALRGA FDRVRGGARR VTSRDPEGAY RALEKYSIDL TARAREGKLD
     PVIGRDTEIR RVVQVLSRRT KNNPVLIGEP GVGKTAIVEG LALRVAAGDV PESLRGRRIV
     SLDLGSMVAG SKLRGEFEER LTSVLTEIRE AEGQIITFID ELHTVVGAGA AEGAMDAGNM
     LKPMLARGEL RMIGATTLDE YRSRIEKDPA LERRFQPVMV GEPSVEDTIG ILRGLKERYE
     VHHGVRITDS ALVAAATLSD RYVTARFLPD KAIDLVDEAA SRLRMEIDSR PVAVDELERA
     VRRLEIEDMA LSKENDDASR QRRERLQREL AEKREELSAL TARWQREKNS ISEVQKIKEE
     LENARRAAEM AERDLDLAKA GELRYGTIPT LEKRLAAATD ALAGSDSPGG AMLSEEVGPD
     DVAEVVASWT GIPAGRMLEG ETAKLLRMEE ELHRRVIGQD DAVRIVSDAV RRARAGIADP
     DRPTGSFLFL GPTGVGKTEL AKAVADFLFD DERAVVRIDM SEYAEKHSVA RLIGAPPGYV
     GFESGGQLTE AIRRRPYSVI LLDEVEKAHP DVFDVLLAVL DDGRLTDGQG RTVDFRNTIL
     ILTSNLGSAF IADPTLPPQV RRDSVMVAVR DAFKPEFLNR LDDVLVFEQL GREDLTRIVD
     IQIDRLRRRL ADRRIDLTVT DAAKGWLADA GYDPVYGARP LRRLVQTSIG DQLAREILAG
     EIRDGNEVVV DVDPKRSALT VHPTVGAPAI
//
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