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PangenomeCOLN315NCTC8325NewmanUSA300_FPR375704-0298108BA0217611819-97685071193ECT-R 2ED133ED98HO 5096 0412JH1JH9JKD6008JKD6159LGA251M013MRSA252MSHR1132MSSA476MW2Mu3Mu50RF122ST398T0131TCH60TW20USA300_TCH1516VC40
⊟Summary[edit | edit source]
- pan ID?: SAUPAN001416000
- symbol?: dut
- synonym:
- description?: dUTP pyrophosphatase
- dUTP pyrophosphatase
- bacteriophage L54a deoxyuridine 5-triphosphate nucleotidohydrolase
- dUTP diphosphatase
- prophage L54a, deoxyuridine 5'-triphosphate nucleotidohydrolase
- bacteriophage L54a, deoxyuridine 5-triphosphate nucleotidohydrolase
- deoxyuridine 5'-triphosphate nucleotidohydrolase
- putative dUTP pyrophosphatase
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 1692283..1692795
- synteny block?: BlockID0008950
- occurrence?: in 27% of 33 strains
dut : prophage trimeric dUTP pyrophosphatase [1]
All staphylococcal prophages produce a deoxyuridine triphosphate pyrophosphatase to ensure uridines are not mistakenly incorporated into phage DNA. dUTP pyrophosphatases are common targets of CRISPR antiphage defense systems so there is a powerful evolutionary pressure for prophage dUTPase structural diversity. Interestingly, completely structurally-distinct dUTPases can all de-repress stlSaPIbov1-regulated pathogenicity islands, providing a defense against superinfection.
⊟Orthologs[edit | edit source]
04-02981:
—
08BA02176:
—
11819-97:
MS7_1480 (dut)
6850:
—
71193:
ST398NM01_2935
ECT-R 2:
—
ED133:
SAOV_1092
ED98:
SAAV_0845
HO 5096 0412:
—
JH1:
—
JH9:
—
JKD6008:
—
JKD6159:
—
LGA251:
—
M013:
—
MRSA252:
—
MSHR1132:
SAMSHR1132_18150
MSSA476:
—
Mu3:
—
Mu50:
—
MW2:
—
RF122:
—
ST398:
—
T0131:
—
TCH60:
—
TW20:
—
USA300_TCH1516:
USA300HOU_1980 (dut)
VC40:
—
⊟Genome Viewer[edit | edit source]
COL | |
NCTC8325 | |
USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MTNTLQVKLLSKNARMPERNHKTDAGYDIFSAETVVLEPQEKAVIKTDVAVSIPEGYVGL
NCTC8325 MTNTLQVKLLSKNARMPERNHKTDAGYDIFSAETVVLEPQEKAVIKTDVAVSIPEGYVGL
USA300_FPR3757 MTNILQVKLLSENARMPERNHKTDAGYDIFSAETVVLEPQEKAVIKTDVAVSIPEGYVGL
*** *******:************************************************
COL LTSRSGVSSKTYLVIETGKIDAGYHGNLGINIKND------EERDGIPFLYDDIDAELED
NCTC8325 LTSRSGVSSKTYLVIETGKIDAGYHGNLGINIKND------EERDGIPFLYDDIDAELED
USA300_FPR3757 LTSRSGVSSKTHLVIETGKIDAGYHGNLGINIKNDNETLESEDMSNFGRSPAGIDGKYAR
***********:*********************** *: ..: .**.:
COL GLIS--ILDIKGNYVQDGRGIRRVYQINKGDKLAQLVIVPIWTPELKQVEEFESVSERGA
NCTC8325 GLIS--ILDIKGNYVQDGRGIRRVYQINKGDKLAQLVIVPIWTPELKQVEEFESVSERGA
USA300_FPR3757 LPVTDKILCMNGSYV-----------INKGDKLAQLVIVPIWTPELKQVEEFESVSERGA
:: ** ::*.** **********************************
COL KGFGSSGV
NCTC8325 KGFGSSGV
USA300_FPR3757 KGFGSSGV
********
- ↑ María Angeles Tormo-Más, Ignacio Mir, Archana Shrestha, Sandra M Tallent, Susana Campoy, Iñigo Lasa, Jordi Barbé, Richard P Novick, Gail E Christie, José R Penadés
Moonlighting bacteriophage proteins derepress staphylococcal pathogenicity islands.
Nature: 2010, 465(7299);779-82
[PubMed:20473284] [WorldCat.org] [DOI] (I p)Janine Bowring, Maan M Neamah, Jorge Donderis, Ignacio Mir-Sanchis, Christian Alite, J Rafael Ciges-Tomas, Elisa Maiques, Iltyar Medmedov, Alberto Marina, José R Penadés
Pirating conserved phage mechanisms promotes promiscuous staphylococcal pathogenicity island transfer.
Elife: 2017, 6;
[PubMed:28826473] [WorldCat.org] [DOI] (I e)