ID A0A5R9LQ46_9ACTN Unreviewed; 867 AA.
AC A0A5R9LQ46;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:QNA78126.1};
GN ORFNames=C8250_023510 {ECO:0000313|EMBL:QNA78126.1};
OS Streptomyces sp. So13.3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2136173 {ECO:0000313|EMBL:QNA78126.1, ECO:0000313|Proteomes:UP000310490};
RN [1] {ECO:0000313|EMBL:QNA78126.1, ECO:0000313|Proteomes:UP000310490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So13.3 {ECO:0000313|EMBL:QNA78126.1,
RC ECO:0000313|Proteomes:UP000310490};
RX PubMed=31097761; DOI=.1038/s41598-019-43960-7;
RA Nunez-Montero K., Lamilla C., Abanto M., Maruyama F., Jorquera M.A.,
RA Santos A., Martinez-Urtaza J., Barrientos L.;
RT "Antarctic Streptomyces fildesensis So13.3 strain as a promising source for
RT antimicrobials discovery.";
RL Sci. Rep. 9:7488-7488(2019).
RN [2] {ECO:0000313|EMBL:QNA78126.1, ECO:0000313|Proteomes:UP000310490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So13.3 {ECO:0000313|EMBL:QNA78126.1,
RC ECO:0000313|Proteomes:UP000310490};
RX PubMed=32349314;
RA Nunez-Montero K., Quezada-Solis D., Khalil Z.G., Capon R.J., Andreote F.D.,
RA Barrientos L.;
RT "Genomic and Metabolomic Analysis of Antarctic Bacteria Revealed Culture
RT and Elicitation Conditions for the Production of Antimicrobial Compounds.";
RL Biomolecules 10:E673-E673(2020).
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; CP048835; QNA78126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5R9LQ46; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000310490; 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:UP000310490};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Stress response {ECO:0000256|RuleBase:RU362034}.
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 94273 MW; 95C349573C3391F7 CRC64;
MEAELTNKSR EALNTANAHA VSAGNPDLTP AHLLLALLGG ADNENIVDLM AAVGADAAEL
RAGTERLIAA LPVVQGATVA PPQANRDLLA VVADASQRAK DLGDDYISTE HLLIGIAVKG
GQAGELLVQR GATAKKLLDA FESARGGQRV TSQDPEGTYK ALEKYGTDFT AAAREGKLDP
VIGRDQEIRR VVQVLSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP ESLRNKRLVS
LDLGAMVAGA KYRGEFEERL KAVLSEIKES DGRVITFIDE LHTVVGAGAG GDSAMDAGNM
LKPMLARGEL RMVGATTLDE YRERIEKDPA LERRFQQVMV AEPSVEDTIA ILRGLKGRYE
AHHKVQIADS ALVAAATLSN RYITSRFLPD KAIDLVDEAA SRLRMEIDSS PVAIDELQRA
VDRLRMEEMA LKNETDPASV QRLEKLRKDL ADKEEELRGL TARWEKEKEG LNRVGAIKES
LDEVNTDIER AQRDGDFEAA SKLLYGEKPR LEAELAEATE AEAAAAKDTM VKDEVGPDDI
ADVVGAWTGI PAGRLLEGET QKLLRMEDEL GRRLIGQTEA VRSVSDAVRR SRSGISDPDR
PTGSFLFLGP TGVGKTELAK ALADFLFDDE RAMVRIDMSE YGEKHSVARL VGAPPGYVGY
EEGGQLTEAV RRRPYSVVLL DEVEKAHHDV FDVLLQVLDD GRLTDGQGRT VDFRNAILIL
TSNLGSQYLV DPVLGDAEKK QSVLETVRMS FKPEFLNRLD DIVVFSALNK EELRHIARLQ
TDRLADRLRD RRLVLDVTDA ALDWLADEGN DPAYGARPLR RLVQTAIGDP LARAILSGEV
VDGDTVRVDR AGEGLIVGPA PSLSKTV
//