ID A0A1H1DGC5_9ACTN Unreviewed; 865 AA.
AC A0A1H1DGC5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04489764_1969 {ECO:0000313|EMBL:SDQ74906.1};
OS Thermostaphylospora chromogena.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermostaphylospora.
OX NCBI_TaxID=35622 {ECO:0000313|EMBL:SDQ74906.1, ECO:0000313|Proteomes:UP000217103};
RN [1] {ECO:0000313|EMBL:SDQ74906.1, ECO:0000313|Proteomes:UP000217103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43794 {ECO:0000313|EMBL:SDQ74906.1,
RC ECO:0000313|Proteomes:UP000217103};
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; FNKK01000002; SDQ74906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1DGC5; -.
DR STRING; 35622.SAMN04489764_1969; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000217103; 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:SDQ74906.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDQ74906.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217103};
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 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 94893 MW; 3D29C201405F336F CRC64;
MDYKLTKKSQ EAVSAAIRRA AAEGNPEVAP AHLFTALLSQ TGGTAVPLLE AVGADWRSLR
AEAERQLERL PKAQGATVSA PTTSRHLLVV LNTAAARAKQ LEDEYVSTEH LLVGLAADGG
PIADLLKSKG ATPEALLDAF EKVRGHARVT SETPEDTYQA LEKYGVDLTE RARAGKLDPV
IGRDSEIRRV IQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPE SLKNKRLVAL
DLGAMVAGAK YRGEFEERLK AVLSEIKESD GQIITFIDEL HTVVGAGAAE GAMDAGNMLK
PMLARGELRM IGATTLDEYR ERIEKDPALE RRFQQIYVGE PSVEDTIAIL RGLKGRYEAH
HQVQIADSAM VAAATLSDRY ITSRFLPDKA IDLVDEAASR LRMEIDSRPV EIDELQRTVD
RLKMEELALA KETDEASRTR LEKLRKELAD RQEELNALVA RWEREKAGLN RVGELKKQLD
EARSAAERAQ RDGDFETASR LMYAEIPQLE KALEEASAQA QPEDAMVKEE VGPDDIAQVV
SSWTGIPTGR LLEGETTKLL RMEDEIGKRI IGQRQAVQAV SDAVRRARAG IADPDRPTGS
FLFLGPTGVG KTELAKALAE FLFDDERAMT RIDMSEYSEK HSVARLVGAP PGYVGYEEGG
QLTEAVRRRP YTVVLLDEVE KAHAEVFDIL LQVLDDGRLT DGQGRTVDFR NTILIMTSNL
GSQYLIDPSM EPQAKRDAVM STVRSAFKPE FLNRLDDIIM FDALGSDELS QIVDLQVDRL
AKRLADRRLT LTVTPAAREW LALTGYDPLY GARPLRRLVQ SAIGDKLAKK VLSGEIVDGD
DVVVELDEAG DTLTVKAKSL VPEAG
//
