ID A0A1I5LVT9_9ACTN Unreviewed; 863 AA.
AC A0A1I5LVT9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04489713_11147 {ECO:0000313|EMBL:SFP01385.1};
OS Actinomadura madurae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1993 {ECO:0000313|EMBL:SFP01385.1, ECO:0000313|Proteomes:UP000183413};
RN [1] {ECO:0000313|EMBL:SFP01385.1, ECO:0000313|Proteomes:UP000183413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43067 {ECO:0000313|EMBL:SFP01385.1,
RC ECO:0000313|Proteomes:UP000183413};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOVH01000011; SFP01385.1; -; Genomic_DNA.
DR RefSeq; WP_021595971.1; NZ_FOVH01000011.1.
DR AlphaFoldDB; A0A1I5LVT9; -.
DR STRING; 1993.SAMN04489713_11147; -.
DR eggNOG; COG0542; Bacteria.
DR InParanoid; A0A1I5LVT9; -.
DR Proteomes; UP000183413; 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:SFP01385.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFP01385.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183413};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 84..111
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 412..530
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 94746 MW; 0D21759594F58379 CRC64;
MDYKLTQKSQ EAVSVAVRRA AAEGHPEVDP QHLLVALIGL PDGTAVPLLE AIGADWQVIR
RRAEERLAAM PKAQGSTVAT PRLSGQLQRS INTAANRAQQ LEDEYVSTEH LLVGLAADGG
PAAGLLKEFG ATPQALLDAF EKVRGHARVT TENPEGTYQS LEKYGVDLTG AARDGRLDPV
IGRDSEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPE SLRGKRLVSL
DLSAMVAGAK YRGEFEERLK AVLNEIKESD GRIVTFIDEL HTVVGAGAAE GAMDAGNMLK
PMLARGELRM IGATTLDEYR ERIEKDPALE RRFQQVFVGE PSVEDSIAIL RGLKGRYEAH
HKVQINDSAL VAAATLSDRY ITSRFLPDKA IDLVDEAASR LRMEIDSRPV EIDELQRAVD
RLKMEELNLA KETDEASRQR LDRLRKDLAD KQEQLTGLVA RWDKEKASLN RVGGIKERID
QLRGEAERAQ RDGDLETSAR LTYGEIPALE KQLEEASEDA ENRDAMVKEE VGPDDVADVV
ASWTGIPAGR LLEGETAKLL RMEDELGRRL IGQETAVRTV SDAVRRARAG ISDPDRPTGS
FLFLGPTGVG KTELAKALAE FLFDDERAMT RIDMSEYSEK HSVARLVGAP PGYIGYEEGG
QLTEAVRRRP YSAVLLDEVE KAHPEVFDIL LQVLDDGRLT DGQGRTVDFR NTILILTSNI
GSQFLVDPTL ENGAKREAVW NAVRNSFKPE FLNRLDDVIL FDALSTDELT RIVDLQVDTL
AARLADRRLT LQVTPAAREW LAMTGYDPLY GARPLRRLVQ TAIGDQLARE LLSGGIRDGD
EVIVDLDEAA DALTVHAAKG LTV
//
