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
//