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Database: UniProt
Entry: A0A5R9LQ46_9ACTN
LinkDB: A0A5R9LQ46_9ACTN
Original site: A0A5R9LQ46_9ACTN 
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
//
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