NUCE_STRPN
ID NUCE_STRPN Reviewed; 274 AA.
AC P0A3S3; Q03158;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=DNA-entry nuclease;
DE AltName: Full=Competence-specific nuclease;
DE EC=3.1.30.-;
GN Name=endA; OrderedLocusNames=SP_1964;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=470;
RX PubMed=2359120; DOI=10.1016/s0022-2836(05)80259-1;
RA Puyet A., Greenberg B., Lacks S.A.;
RT "Genetic and structural characterization of endA. A membrane-bound nuclease
RT required for transformation of Streptococcus pneumoniae.";
RL J. Mol. Biol. 213:727-738(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
CC -!- FUNCTION: By degrading DNA that enters the cell, plays a role in the
CC competence of cells to be transformed.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC -!- MISCELLANEOUS: The active site contains 1 hydrated divalent metal
CC cation that has only 1 direct interaction with the protein; all other
CC interactions are via water molecules. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC {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; X54225; CAA38134.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK76031.1; -; Genomic_DNA.
DR PIR; F95229; F95229.
DR PIR; S10641; S10641.
DR RefSeq; WP_001036779.1; NZ_AKVY01000001.1.
DR PDB; 3OWV; X-ray; 1.75 A; A/B=31-274.
DR PDBsum; 3OWV; -.
DR AlphaFoldDB; P0A3S3; -.
DR SMR; P0A3S3; -.
DR STRING; 170187.SP_1964; -.
DR EnsemblBacteria; AAK76031; AAK76031; SP_1964.
DR GeneID; 60233012; -.
DR KEGG; spn:SP_1964; -.
DR eggNOG; ENOG5033PER; Bacteria.
DR OMA; NYYETKI; -.
DR PhylomeDB; P0A3S3; -.
DR BioCyc; SPNE170187:G1FZB-2018-MON; -.
DR PHI-base; PHI:3705; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.570.10; -; 1.
DR InterPro; IPR018524; DNA/RNA_endonuclease_AS.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR SMART; SM00892; Endonuclease_NS; 1.
DR PROSITE; PS01070; NUCLEASE_NON_SPEC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Competence; Endonuclease; Hydrolase; Membrane;
KW Metal-binding; Nuclease; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..274
FT /note="DNA-entry nuclease"
FT /id="PRO_0000178667"
FT TRANSMEM 8..25
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT REGION 29..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10047"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3OWV"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3OWV"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 107..117
FT /evidence="ECO:0007829|PDB:3OWV"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:3OWV"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:3OWV"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:3OWV"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:3OWV"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3OWV"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:3OWV"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3OWV"
SQ SEQUENCE 274 AA; 29891 MW; 59B2243F0150CD98 CRC64;
MNKKTRQTLI GLLVLLLLST GSYYIKQMPS APNSPKTNLS QKKQASEAPS QALAESVLTD
AVKSQIKGSL EWNGSGAFIV NGNKTNLDAK VSSKPYADNK TKTVGKETVP TVANALLSKA
TRQYKNRKET GNGSTSWTPP GWHQVKNLKG SYTHAVDRGH LLGYALIGGL DGFDASTSNP
KNIAVQTAWA NQAQAEYSTG QNYYESKVRK ALDQNKRVRY RVTLYYASNE DLVPSASQIE
AKSSDGELEF NVLVPNVQKG LQLDYRTGEV TVTQ
