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
//