ID   NUC34_STRAT             Reviewed;           9 AA.
AC   P83222;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   12-AUG-2020, entry version 32.
DE   RecName: Full=34 kDa extracellular nuclease;
DE            EC=3.-.-.-;
DE   Flags: Fragment;
OS   Streptomyces antibioticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1890;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=ATCC 11891 / DSM 40868 / BCRC 11580 / NCIMB 11506 / PSA 205;
RX   PubMed=10400660; DOI=10.1074/jbc.274.29.20366;
RA   Nicieza R.G., Huergo J., Connolly B.A., Sanchez J.;
RT   "Purification, characterization, and role of nucleases and serine proteases
RT   in Streptomyces differentiation. Analogies with the biochemical processes
RT   described in late steps of eukaryotic apoptosis.";
RL   J. Biol. Chem. 274:20366-20375(1999).
CC   -!- FUNCTION: Involved in DNA degradation in the substrate mycelium. Cuts
CC       DNA nonspecifically. Possesses endonucleolytic activity.
CC       {ECO:0000269|PubMed:10400660}.
CC   -!- ACTIVITY REGULATION: Stimulated by magnesium and manganese. Inhibited
CC       by zinc and aurin tricarboxylic acid. {ECO:0000269|PubMed:10400660}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8-8.5.;
CC   -!- SUBUNIT: Monomer. {ECO:0000303|PubMed:10400660, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10400660}.
CC   -!- DEVELOPMENTAL STAGE: Highest expression found during aerial mycelium
CC       formation and sporulation. {ECO:0000269|PubMed:10400660}.
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DR   GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR   GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; TAS:UniProtKB.
DR   GO; GO:0006308; P:DNA catabolic process; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Magnesium; Manganese; Nuclease;
KW   Secreted.
FT   CHAIN           1..>9
FT                   /note="34 kDa extracellular nuclease"
FT                   /id="PRO_0000057976"
FT   UNSURE          1
FT                   /note="G or E"
FT   UNSURE          5
FT                   /note="G or A"
FT   NON_TER         9
FT                   /evidence="ECO:0000303|PubMed:10400660"
SQ   SEQUENCE   9 AA;  994 MW;  80B05AB6D8705731 CRC64;
     GTLIGQDYK