ID A0A3E0I8G5_9PSEU Unreviewed; 863 AA.
AC A0A3E0I8G5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BCF44_10128 {ECO:0000313|EMBL:REH55012.1};
OS Kutzneria buriramensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1045776 {ECO:0000313|EMBL:REH55012.1, ECO:0000313|Proteomes:UP000256269};
RN [1] {ECO:0000313|EMBL:REH55012.1, ECO:0000313|Proteomes:UP000256269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45791 {ECO:0000313|EMBL:REH55012.1,
RC ECO:0000313|Proteomes:UP000256269};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (AUG-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|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:REH55012.1}.
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DR EMBL; QUNO01000001; REH55012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E0I8G5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000256269; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:REH55012.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:REH55012.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 93970 MW; E627829EF19E8E88 CRC64;
MNQFNPTTKT QQAVSEAAQA ATMAGNPDIT PVHLLAALLA QGDGLTAPLL TAVGADPAQV
RAELEKLAHS LPSATGATMS APQLSRDGLR VITHAQRLAT EMGDEYVSTE HLLVGLAAEG
GQVADLLRRH GATPDALREA FTKVRGSARI TSPDPEGTFQ ALEKYGVDLT QRARDGELDP
VIGRDAEIRR VVQVLSRRTK NNPVLIGEPG VGKTAIVEGL AQRVVAGDVP ESLRGKRVVA
LDLGSMVAGA KYRGEFEERL KAVLKEITDS DGQVITFIDE LHTIVGAGAT GEGAMDAGNM
IKPMLARGEL RMVGATTLDE YRQHIEKDPA LERRFQQVLV GEPSVEDTIG ILRGLKERYE
VHHGVRITDT ALVAAATLSD RYITARFLPD KAIDLVDEAA SRLRMEIDSR PVEIDEVERA
VRRLEIEEMA LEKESDQASK ERLDALRAEL AEKREELSAL TARWQNEKGS IEKVRELKEQ
LEQLRGESER AERDSDLGRA AELRYGRIPA LEKDLAAATA NTPTGDVMLK EEVGPDDVAD
VVSAWTGIPA GRLLEGETAK LLRMEDELAA RVVGQAEAVR VVSDAVRRTR AGVADPDRPT
GSFLFLGPTG VGKTELAKAL AEFLFDDERA MIRIDMSEYA EKHSVARLVG APPGYVGYDQ
GGQLTESVRR RPYSVVLLDE VEKAHPDVFD VLLQVLDDGR LTDGQGRTVD FRNTILVLTS
NLGSQAIADP VLTEQQRKDA VLATVQRHFK PEFLNRLDDV VVFHALATEE LTQIVDIQVA
RLAKRLAQRR LSLEVSPGAR DWLALNGFDP VYGARPLRRL VQSSIGDQLA KELLAGEIRD
GDTVLVDVVE DNSGLMVGRS LTA
//
