DRNE_VIBCH
ID DRNE_VIBCH Reviewed; 231 AA.
AC P08038; Q9KUP5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Extracellular deoxyribonuclease;
DE Short=DNase;
DE EC=3.1.21.-;
DE Flags: Precursor;
GN Name=dns; OrderedLocusNames=VC_0470;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3036665; DOI=10.1016/0378-1119(87)90090-4;
RA Focareta T., Manning P.A.;
RT "Extracellular proteins of Vibrio cholerae: molecular cloning, nucleotide
RT sequence and characterization of the deoxyribonuclease (DNase) together
RT with its periplasmic localization in Escherichia coli K-12.";
RL Gene 53:31-40(1987).
RN [2]
RP SEQUENCE REVISION.
RA Manning P.A.;
RL Submitted (NOV-1987) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the EndA/NucM nuclease family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M16499; AAA27516.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF93643.1; -; Genomic_DNA.
DR PIR; A26509; A26509.
DR PIR; C82319; C82319.
DR RefSeq; NP_230124.1; NC_002505.1.
DR RefSeq; WP_000972596.1; NZ_LT906614.1.
DR PDB; 2VND; X-ray; 1.70 A; A=1-231.
DR PDBsum; 2VND; -.
DR AlphaFoldDB; P08038; -.
DR SMR; P08038; -.
DR STRING; 243277.VC_0470; -.
DR DNASU; 2615132; -.
DR EnsemblBacteria; AAF93643; AAF93643; VC_0470.
DR GeneID; 57739216; -.
DR KEGG; vch:VC_0470; -.
DR PATRIC; fig|243277.26.peg.443; -.
DR eggNOG; COG2356; Bacteria.
DR HOGENOM; CLU_070541_0_0_6; -.
DR OMA; ADQYGQC; -.
DR BioCyc; VCHO:VC0470-MON; -.
DR EvolutionaryTrace; P08038; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004536; F:deoxyribonuclease activity; IMP:TIGR.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006308; P:DNA catabolic process; IMP:TIGR.
DR InterPro; IPR007346; Endonuclease-I.
DR InterPro; IPR044925; His-Me_finger_sf.
DR PANTHER; PTHR33607; PTHR33607; 1.
DR Pfam; PF04231; Endonuclease_1; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..231
FT /note="Extracellular deoxyribonuclease"
FT /id="PRO_0000007833"
FT CONFLICT 50
FT /note="R -> P (in Ref. 1; AAA27516)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..169
FT /note="PPERARG -> AQSVQR (in Ref. 1; AAA27516)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="S -> T (in Ref. 1; AAA27516)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..228
FT /note="RFVREQ -> LLCACK (in Ref. 1; AAA27516)"
FT /evidence="ECO:0000305"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:2VND"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2VND"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2VND"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2VND"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2VND"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:2VND"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:2VND"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:2VND"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:2VND"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:2VND"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2VND"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2VND"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:2VND"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2VND"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:2VND"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:2VND"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2VND"
FT HELIX 165..182
FT /evidence="ECO:0007829|PDB:2VND"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:2VND"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:2VND"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:2VND"
SQ SEQUENCE 231 AA; 26713 MW; 9E9541460EDE866B CRC64;
MMIFRFVTTL AASLPLLTFA APISFSHAKN EAVKIYRDHP VSFYCGCEIR WQGKKGIPDL
ESCGYQVRKN ENRASRIEWE HVVPAWQFGH QLQCWQQGGR KNCTRTSPEF NQMEADLHNL
TPAIGEVNGD RSNFSFSQWN GVDGVTYGQC EMQVNFKERT AMPPERARGA IARTYLYMSE
QYGLRLSKAQ SQLMQAWNNQ YPVSEWECVR DQRIEKVQGN SNRFVREQCP N