ID A0A117R2U1_9ACTN Unreviewed; 879 AA.
AC A0A117R2U1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=AQJ54_13215 {ECO:0000313|EMBL:KUN67991.1};
OS Streptomyces griseorubiginosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67304 {ECO:0000313|EMBL:KUN67991.1, ECO:0000313|Proteomes:UP000054375};
RN [1] {ECO:0000313|EMBL:KUN67991.1, ECO:0000313|Proteomes:UP000054375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40469 {ECO:0000313|EMBL:KUN67991.1,
RC ECO:0000313|Proteomes:UP000054375};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseorubiginosus DSM 40469, type
RT strain for the species Streptomyces griseorubiginosus.";
RL Submitted (OCT-2015) 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}.
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:KUN67991.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMWV01000007; KUN67991.1; -; Genomic_DNA.
DR RefSeq; WP_062237281.1; NZ_KQ948736.1.
DR AlphaFoldDB; A0A117R2U1; -.
DR Proteomes; UP000054375; 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:UP000054375};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 87..121
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 417..538
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 879 AA; 98011 MW; 86AB356EA7E14FCD CRC64;
MDMNRLTQKS QEALQEAQSV AVGLGQTEVD GEHLLLALLD QEDGLIPRLL QQAGARPEEL
RAAVQGDLSR RPKVTGPGAA PGQVFVTQRL SRLLDAAERE AKRLKDEYVS VEHLLLALAE
EGSATAAGRL LKEHGVTRDS FLSALTQVRG NQRVTSANPE VAYEALEKYG RDLVLEARSG
RLDPVIGRDA EIRRVTQILS RKTKNNPVLI GDPGVGKTAI VEGLAQRIVR GDVPEGLRDR
TVFALDMGSL VAGAKYRGEF EERLKAVLSE VKAAQGRILL FVDELHTVVG AGAAEGAMDA
GNMLKPMLAR GELHMIGATT LDEYRKHIEK DAALERRFQQ VLVDEPSVED TISILRGLRE
RLEVFHGVKI QDTALVSAAT LSHRYITDRF LPDKAIDLVD EACARLRTEI DSMPAELDEI
TRRVTRLEIE EAALSKETDA ASKARLEELR RELADLRGEA DAKHAQWEAE RQAIRRVQEL
RQELEQARHE AEEAERVYDL NRAAELRYGR LQDLERRLAA EEEQLAAKQG QNRLLREVVT
EEEIAQIVAA WTGVPVARLQ EGEREKLLRL DEILRERVIG QDEAVKLVAD AIIRARSGIR
DPRRPIGSFI FLGPTGVGKT ELAKTLAAAL FDSEENMVRL DMSEYQERHT VSRLMGAPPG
YVGYEEGGQL TEAVRRKPYS VVLFDEIEKA HTDVFNTLLQ VLDDGRITDS QGRTVDFRNT
VIIMTSNIGS EHLLDGATAD GEIKPDARAL VTGELRGHFR PEFLNRVDDI VLFKPLGERQ
IERIVELQFD ELRRRLAERR IAVELTDSAR ELIAHQGYDP VYGARPLRRY ISHEVETMVG
RALLRGDVQD GATVRVDAAH GELVVTYDRP EDVKGVRAA
//
