ID A0A4R4S7J2_9ACTN Unreviewed; 865 AA.
AC A0A4R4S7J2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TDC57949.1};
GN ORFNames=E1281_03320 {ECO:0000313|EMBL:TDC57949.1};
OS Actinomadura sp. KC345.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2530371 {ECO:0000313|EMBL:TDC57949.1, ECO:0000313|Proteomes:UP000295623};
RN [1] {ECO:0000313|EMBL:TDC57949.1, ECO:0000313|Proteomes:UP000295623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KC345 {ECO:0000313|EMBL:TDC57949.1,
RC ECO:0000313|Proteomes:UP000295623};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequences of novel Actinobacteria.";
RL Submitted (FEB-2019) 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:TDC57949.1}.
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DR EMBL; SMKH01000010; TDC57949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R4S7J2; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000295623; 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:UP000295623};
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..439
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 472..530
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 94698 MW; F92DA25230877C3B CRC64;
MDYKLTQKSQ EAVSVAVRRA AAEGHPEVEP QHLLVALIGL ADGTAVPLLE AVGADWQAIR
RQAEEQLAAK PKAQGSTVAT PRLSGQLQRS INTAANRAKR LEDDYVSTEH LLVGLAADGG
PAAGLLKEFG ATPEALLDAF EKVRGHARVT SENPEGTYQS LEKYGVDLTA AARDGRLDPV
IGRDSEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIIAGDVPE SLRGKKLVSL
DLSAMVAGAK YRGEFEERLK AVLHEIKESE GQIVTFIDEL HTVVGAGAAE GAMDAGNMLK
PMLARGELRM IGATTLDEYR ERIEKDAALE RRFQQVFVGE PTVEDTIAIL RGLKGRYEAH
HKVQINDSAL VSAAALSDRY ITSRYLPDKA IDLVDEAASR LRMEIDSRPV EIDELQRTVD
RLKMEEMNLS KETDEASRQR LDRLRADLAD KQEHLTGLVA RWDKEKASLN RVGAIKERID
QLHGEAERAQ RDGDLETSAR LSYGEIPELE KQLEEASEAA ENRDAMVKEE VGPDDVADVV
ASWTGIPAGR LLEGETAKLL RMEDELGRRL IGQATAVRTV SDAVRRARAG ISDPDRPTGS
FLFLGPTGVG KTELAKALAE FLFDDERAIT RIDMSEYSEK HSVARLVGAP PGYVGYEEGG
QLTEAVRRRP YSAVLLDEVE KAHPEVFDIL LQVLDDGRLT DGQGRTVDFR NTILILTSNI
GSQFLVDPTL ENGAKREAVW NAVRNAFKPE FLNRLDDVIL FDALSTAELT KIVDLQVDAL
AGRLAERQLT LNVSDAAREW LALTGYDPLY GARPLRRLVQ TAIGDQLARE LLSGEVRDGD
EVVVDLDEAA DKLTVAPAQG LTLTK
//
