ID   DNAS1_THISK             Reviewed;         361 AA.
AC   D3SGB1;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Deoxyribonuclease {ECO:0000303|PubMed:26191053};
DE            Short=DNase {ECO:0000303|PubMed:26191053};
DE            EC=3.1.-.- {ECO:0000305|PubMed:26191053};
DE   Flags: Precursor;
GN   ORFNames=TK90_2665 {ECO:0000312|EMBL:ADC73152.1};
OS   Thioalkalivibrio sp. (strain K90mix).
OG   Plasmid pTK9001 {ECO:0000312|EMBL:ADC73152.1,
OG   ECO:0000312|Proteomes:UP000009099}.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio; unclassified Thioalkalivibrio.
OX   NCBI_TaxID=396595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K90mix {ECO:0000312|EMBL:ADC73152.1}; PLASMID=pTK9001;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.;
RT   "Complete sequence of plasmid of Thioalkalivibrio sp. K90mix.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, COFACTOR, DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-149
RP   AND 283-ASN--PRO-361, 3D-STRUCTURE MODELING, AND ACTIVE SITE.
RC   STRAIN=K90mix;
RX   PubMed=26191053; DOI=10.3389/fmicb.2015.00661;
RA   Alzbutas G., Kaniusaite M., Grybauskas A., Lagunavicius A.;
RT   "Domain organization of DNase from Thioalkalivibrio sp. provides insights
RT   into retention of activity in high salt environments.";
RL   Front. Microbiol. 6:661-661(2015).
CC   -!- FUNCTION: DNA nuclease able to digest short and long DNA substrate. Is
CC       resistant to ionic strength and thus active at high salt concentration.
CC       {ECO:0000269|PubMed:26191053}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:26191053};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:26191053};
CC       Note=Requires Ca(2+) or Mg(2+) for catalytic activity and the maximum
CC       activity is achieved when both of these ion species are present.
CC       {ECO:0000269|PubMed:26191053};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26191053}.
CC   -!- DOMAIN: Harbors two domains: an N-terminal domain, that exhibits DNase
CC       activity, and a C-terminal domain, comprising a duplicate DNA binding
CC       helix-hairpin-helix motif. The C-terminal domain is responsible for the
CC       enzyme's resistance to high ionic strength, it acts as a facilitator
CC       for DNA binding at high salt concentrations.
CC       {ECO:0000269|PubMed:26191053}.
CC   -!- MISCELLANEOUS: Thioalkalivibrio sp. K90mix is adapted to extreme salt
CC       concentrations and grows at salinities up to 4 M of NaCl.
CC       {ECO:0000305|PubMed:26191053}.
CC   -!- SIMILARITY: Belongs to the DNase I family.
CC       {ECO:0000305|PubMed:26191053}.
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DR   EMBL; CP001906; ADC73152.1; -; Genomic_DNA.
DR   RefSeq; WP_013006517.1; NC_013930.1.
DR   AlphaFoldDB; D3SGB1; -.
DR   SMR; D3SGB1; -.
DR   STRING; 396595.TK90_2665; -.
DR   EnsemblBacteria; ADC73152; ADC73152; TK90_2665.
DR   KEGG; tkm:TK90_2665; -.
DR   eggNOG; COG1555; Bacteria.
DR   eggNOG; COG3568; Bacteria.
DR   HOGENOM; CLU_065121_0_0_6; -.
DR   OMA; RYAFIWK; -.
DR   OrthoDB; 439958at2; -.
DR   Proteomes; UP000009099; Plasmid pTK9001.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004536; F:deoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006308; P:DNA catabolic process; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   Gene3D; 3.60.10.10; -; 1.
DR   InterPro; IPR016202; DNase_I.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR010994; RuvA_2-like.
DR   SMART; SM00476; DNaseIc; 1.
DR   SMART; SM00278; HhH1; 2.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF56219; SSF56219; 1.
PE   1: Evidence at protein level;
KW   Calcium; DNA-binding; Hydrolase; Magnesium; Nuclease; Plasmid;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..361
FT                   /note="Deoxyribonuclease"
FT                   /id="PRO_5000576882"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000305|PubMed:26191053"
FT   MUTAGEN         149
FT                   /note="H->A: Loss of catalytic activity, is unable to
FT                   digest DNA at any of the tested concentrations of NaCl."
FT                   /evidence="ECO:0000269|PubMed:26191053"
FT   MUTAGEN         283..361
FT                   /note="Missing: Retains DNase activity, but this mutant
FT                   noticeably digests the DNA substrate only up to 0.6 M NaCl
FT                   and the DNA digestion is completely inhibited at NaCl
FT                   concentrations higher than 1.2 M."
FT                   /evidence="ECO:0000269|PubMed:26191053"
SQ   SEQUENCE   361 AA;  40497 MW;  13DD66415D55E74E CRC64;
     MMHLLRRGAF AILLIVLLPS AALADLRLAS WNIQHLGWNV GKDYPAVARI AAQFDFLAIQ
     EVMNAEGIYR LRDTLEDATG AEWSVLYSDA LGRNTYREKY AFLWREAAVE YVGGALTYID
     EADRFAREPF SAVFRSRGTD QHFLAATVHI TYGDRVADRV EEIEALRRYW DWLADVMPEY
     AGERILFGDF NLPPHHDGWA SMRAVAEPLV TEGATTLSTH DRRYANLYDN LWVPKDHTLP
     LGDAGILPFP VVLSEVTGVY WDHEKARDRV SDHAPVYVLF EGNTLHDAVV AEIADQEAGC
     IDLNRASVSE LTALPHIGEA RAEAIKDGRP WNAVRDLKEI RGIGAGRLEE IKARGEACIE
     P