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Database: UniProt
Entry: A0A3M0GLG6_9ACTN
LinkDB: A0A3M0GLG6_9ACTN
Original site: A0A3M0GLG6_9ACTN 
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
//
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