ID A0A3M0GLG6_9ACTN Unreviewed; 858 AA.
AC A0A3M0GLG6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RMB62483.1};
GN ORFNames=EAX62_05315 {ECO:0000313|EMBL:RMB62483.1};
OS Tessaracoccus antarcticus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=2479848 {ECO:0000313|EMBL:RMB62483.1, ECO:0000313|Proteomes:UP000275256};
RN [1] {ECO:0000313|EMBL:RMB62483.1, ECO:0000313|Proteomes:UP000275256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDX10 {ECO:0000313|EMBL:RMB62483.1,
RC ECO:0000313|Proteomes:UP000275256};
RA Zhou L.Y., Du Z.J.;
RT "Tessaracoccus antarcticuss sp. nov., isolated from sediment.";
RL Submitted (OCT-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|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:RMB62483.1}.
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DR EMBL; REFW01000001; RMB62483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0GLG6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000275256; 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 104; 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:UP000275256};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 858 AA; 93270 MW; 89A38FA2B9E8257E CRC64;
MNTEKLTTKS RDAVTSAVRQ ALTNGNPSAE PAHLLHGMLL VPDNTVGPLL ESVGADPHAI
DASAVAAIGK LPSSTGSSVT QPTLSGAFAR VLASAETLAD TLGDQFVATE HLLIALVDVQ
SEASQALKAA GVDSDVLTAA FNGSRGGKRV TSAESEGGES ALDKYSMDLT EQARSGKLDP
VIGRDAEIRR VVQVLARRTK NNPVLIGEPG VGKTAVVEGL ALRLVEGDVP DSLRGRRLVS
LDLASMVAGA KYRGEFEERL KAVLNEIRDA DGQIITFIDE LHTVVGAGAS GEGAMDAGNM
LKPMLARGEL RMIGATTLDE FRERIEKDPA LERRFQQVFV GEPSVEDTVA ILRGLRERYE
AHHKVRITDS ALVAAATLSD RYITSRQLPD KAIDLIDESA SRLRMEIDSS PEEIDMLRRD
VDRMTMQAFA LEKEDDDASR ERLSALRQEL ADAQESLRGL ETTWEAEKAS LNRVGDIKEQ
IDQLRMEADK AQRSGDLTRA SQILYGDIPA AQRELTEAEE KDNTPSMVSE EVSEFDIAEV
VAAWTGVPVG RLLQGEAEKL LQMEQRIGER LIGQRPAVTA VADAVRRSRA GISDPHRPTG
SFLFLGPTGV GKTELAKSLA DFLFDDETAL VRIDMSEYSE KHSVARLVGA PPGYVGYEEG
GQLTEAVRRR PYSVVLLDEV EKAHPDLFNI LLQVLDDGRL TDGQGRTVDF RNTILIMTSN
IGSQYLADAT LDPAGTKDAV MALVRKAFRP EFLNRLDDIV LFDPLTRDEL GRIVEIQLAR
LNRRLVSRRI TVEVSEAAEQ WLGSTGFDPV YGARPLRRLV QTTIEDALAR GLLSGEIHDG
QTVRFDAKPD GSGITLVA
//