ID A0A1R4I866_9ACTN Unreviewed; 860 AA.
AC A0A1R4I866;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=FM114_00380 {ECO:0000313|EMBL:SJN15978.1};
OS Luteococcus japonicus LSP_Lj1.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Luteococcus.
OX NCBI_TaxID=1255658 {ECO:0000313|EMBL:SJN15978.1, ECO:0000313|Proteomes:UP000188342};
RN [1] {ECO:0000313|EMBL:SJN15978.1, ECO:0000313|Proteomes:UP000188342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSP_Lj1 {ECO:0000313|EMBL:SJN15978.1,
RC ECO:0000313|Proteomes:UP000188342};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; FUKQ01000001; SJN15978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4I866; -.
DR STRING; 1255658.FM114_00380; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000188342; 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 78, MITOCHONDRIAL; 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:UP000188342};
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 436..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 860 AA; 94141 MW; 5D1AB879798B1C82 CRC64;
MDTEKLTTMS RDALSAALRN ALANGNPNAE PVHLLHALLL VPDNTVAPLL ASIDVDPTAI
STAAQAAIKK LPSAQGNSVS QPQLSGALAR VLADAELRAD ELGDSYVSTE HLLLALTAVT
SDASKILMDA GATVDKLTKA FNDSRGDRRI TSPEAEGGES ALGKYSVDLT ERARDGKLDP
VIGRDQEIRR VVQVLARRTK NNPVLIGEPG VGKTAVVEGL AQRVVAGDVP DSLKGRRVVS
LDLSSMVAGA KYRGEFEERL KAVLKEIKDA EGQIITFIDE LHTVVGAGAG GEGAMDAGNM
LKPMLARGEL RMIGATTLDE YREHIEKDPA LERRFQQVYV GEPTVEDTIA ILRGLRERYE
AHHKVRITDS ALVAAASLSN RYITNRQLPD KAIDLIDEAA SRLRMEIDSS PEEIDVLRRQ
VDRMKMEQFA VEKETDAASK ARLERLNQEL ADAEEELRAL EARWESEKAG LNRVGDLKTE
IDKLRGEAER FQREGDLAKA AEIQYGRIPA LEKELEEASA AEAEQQRTSM VSEEVASADI
AEVVSAWTGI PVGKMLQGES EKLLHMEDHI GQRLIGQKQA VTAVADAVRR SRAGISDPNR
PTGSFLFLGP TGVGKTELAK SLADFLFDDE TAMVRIDMSE YSEKHSVSRL VGAPPGYVGY
EEGGQLTEAV RRRPYSVVLL DEVEKAHPDL FNILLQVLDD GRLTDGQGRT VDFRNTILIL
TSNLGSQFLA DQNLAKDAKR DAVMGVVRGA FRPEFLNRLD EIVMFDPLTQ EDLTHIVETN
LSKINNRLAE RRIKINVTDE GKEWLARAGF DPVYGARPLR RLVQTTVEDQ MARKLLAGQI
ADGDEVTFDV DESGDGLRIV
//