53DR_STAES
ID 53DR_STAES Reviewed; 179 AA.
AC Q8CTG7;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Putative 5'(3')-deoxyribonucleotidase;
DE EC=3.1.3.-;
GN OrderedLocusNames=SE_0505;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of
CC deoxyribonucleotides. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q97JQ5};
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000305}.
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DR EMBL; AE015929; AAO04102.1; -; Genomic_DNA.
DR RefSeq; NP_764060.1; NC_004461.1.
DR RefSeq; WP_002468869.1; NZ_WBME01000015.1.
DR PDB; 3BWV; X-ray; 1.55 A; A/B=1-179.
DR PDBsum; 3BWV; -.
DR AlphaFoldDB; Q8CTG7; -.
DR SMR; Q8CTG7; -.
DR DNASU; 1056034; -.
DR EnsemblBacteria; AAO04102; AAO04102; SE_0505.
DR KEGG; sep:SE_0505; -.
DR PATRIC; fig|176280.10.peg.477; -.
DR eggNOG; COG4502; Bacteria.
DR HOGENOM; CLU_111510_0_0_9; -.
DR OMA; FNAKFRW; -.
DR EvolutionaryTrace; Q8CTG7; -.
DR Proteomes; UP000001411; Chromosome.
DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR010708; 5'(3')-deoxyribonucleotidase.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF06941; NT5C; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..179
FT /note="Putative 5'(3')-deoxyribonucleotidase"
FT /id="PRO_0000164386"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 11
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:3BWV"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:3BWV"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007744|PDB:3BWV"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3BWV"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:3BWV"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:3BWV"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3BWV"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:3BWV"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3BWV"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:3BWV"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:3BWV"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3BWV"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:3BWV"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3BWV"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3BWV"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3BWV"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:3BWV"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:3BWV"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:3BWV"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3BWV"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3BWV"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:3BWV"
SQ SEQUENCE 179 AA; 20993 MW; 9A5BA6437DE45A6A CRC64;
MTRQRIAIDM DEVLADTLGA VVKAVNERAD LNIKMESLNG KKLKHMIPEH EGLVMDILKE
PGFFRNLDVM PHAQEVVKQL NEHYDIYIAT AAMDVPTSFH DKYEWLLEYF PFLDPQHFVF
CGRKNIILAD YLIDDNPKQL EIFEGKSIMF TASHNVYEHR FERVSGWRDV KNYFNSIEK