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Database: UniProt
Entry: A0A3G8JTC6_9ACTN
LinkDB: A0A3G8JTC6_9ACTN
Original site: A0A3G8JTC6_9ACTN 
ID   A0A3G8JTC6_9ACTN        Unreviewed;       850 AA.
AC   A0A3G8JTC6;
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|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:AZG47772.1};
GN   ORFNames=D7316_04384 {ECO:0000313|EMBL:AZG47772.1};
OS   Gordonia insulae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=2420509 {ECO:0000313|EMBL:AZG47772.1, ECO:0000313|Proteomes:UP000271469};
RN   [1] {ECO:0000313|EMBL:AZG47772.1, ECO:0000313|Proteomes:UP000271469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS17-SY073 {ECO:0000313|EMBL:AZG47772.1,
RC   ECO:0000313|Proteomes:UP000271469};
RA   Kim Y.S., Kim S.B.;
RT   "Gordonia insulae sp. nov., isolated from an island soil.";
RL   Submitted (NOV-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}.
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DR   EMBL; CP033972; AZG47772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G8JTC6; -.
DR   KEGG; gom:D7316_04384; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000271469; Chromosome.
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:UP000271469};
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          413..500
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   850 AA;  92012 MW;  FC692AF21FE764D0 CRC64;
     MDSFNPTTKT QAALSAAVQA AAAAGNSDVR PAHILVALLD QSDGIAAPLL KAVGVDPSTV
     RAQAQGLVDR APTVASASAQ PQLSRESIAA ITAAQQLAGE LDDEYVSTEH ILVGLATGDS
     DTAKLLANVG ATPQALREAF VSVRGNARVT TPDPEQTYQA LEKYSTDLTA AAREGKLDPV
     IGRDTEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIIAGDVPE SLRGKTVISL
     DLGSMVAGAK YRGEFEERLK AVLDEIKGSA GQVITFIDEL HTIVGAGATG DSAMDAGNMI
     KPMLARGELR LVGATTLEEY RQYIEKDAAL ERRFQQVYVG EPSVEDTIGI LRGLKDRYEV
     HHGVRITDSA LVLAATLSDR YITSRFLPDK AIDLVDEAAS RLRMEIDSRP VEIDEVERIV
     RRLEVEEVAL EKETDAASKE RLEKLRGELA DQKEKLNELS ARWQSEKTAI DAVRDVKEEL
     ERLRGEADRA ERESDLGRAA ELRYGKIPAL EKELAAALEK TGADPDQDVM LQEEVGPDDV
     AQVVSAWTGI PAGRMLEGET AKLLRMEDEL GQRVIGQKDA VQAVSDAVRR ARAGVADPNR
     PLGSFLFLGP TGVGKTELAK ALAEFLFDDE RAMVRIDMSE YGEKHSVARL VGAPPGYVGY
     ESGGQLTEAV RRRPYTVVLF DEVEKAHPDV FDVLLQVLDE GRLTDGQGRT VDFRNTILIL
     TSNLGSGGDK DQVMAAVRAA FKPEFINRLD DVVIFDALSP EELVSIVDIQ LAQLGKRLAQ
     RRLELQVTPK AKEWLAERGF DALYGARPLR RLVQQAIGDQ LARALLSGDI HDGDVVPVNV
     GADGESLVLG
//
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