NUCE_STRR6
ID NUCE_STRR6 Reviewed; 274 AA.
AC P0A3S4; Q03158;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=DNA-entry nuclease;
DE AltName: Full=Competence-specific nuclease;
DE EC=3.1.30.-;
GN Name=endA; OrderedLocusNames=spr1779;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
CC -!- FUNCTION: By degrading DNA that enters the cell, plays a role in the
CC competence of cells to be transformed. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
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}.
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DR EMBL; AE007317; AAL00582.1; -; Genomic_DNA.
DR PIR; A99094; A99094.
DR RefSeq; NP_359371.1; NC_003098.1.
DR RefSeq; WP_001036779.1; NC_003098.1.
DR AlphaFoldDB; P0A3S4; -.
DR SMR; P0A3S4; -.
DR STRING; 171101.spr1779; -.
DR EnsemblBacteria; AAL00582; AAL00582; spr1779.
DR GeneID; 60233012; -.
DR KEGG; spr:spr1779; -.
DR PATRIC; fig|171101.6.peg.1920; -.
DR eggNOG; ENOG5033PER; Bacteria.
DR HOGENOM; CLU_080962_0_0_9; -.
DR OMA; NYYETKI; -.
DR Proteomes; UP000000586; 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 3: Inferred from homology;
KW Cell membrane; Competence; Endonuclease; Hydrolase; Membrane;
KW Metal-binding; Nuclease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..274
FT /note="DNA-entry nuclease"
FT /id="PRO_0000178668"
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"
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