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⊟Summary[edit | edit source]
- pan ID?: SAUPAN005029000
- symbol?: ami
- synonym:
- description?: amidase
- amidase
- CHAP domain-containing protein
- autolysin
- bacteriophage autolysin amidase, putative
- lytic enzyme
- phage amidase
- CHAP domain protein
- CHAP protein
- N-acetylmuramoyl-L-alanine amidase
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 5198406..5199161
- synteny block?: BlockID0039100
- occurrence?: in 68% of 34 strains
ami : prophage amidase endolysin [1]
Once prophage have assembled and replicated, they need to emerge from the host cell to infect neighbors. Once prophage holins generate weaknesses in the cell membrane, phage amidase endolysins can access the cell membrane-proximal side of the peptidoglycan cell wall, depolymerize the barrier and promote virion release.
⊟Orthologs[edit | edit source]
04-02981:
SA2981_1906
08BA02176:
—
11819-97:
MS7_1980
6850:
RSAU_000616
71193:
—
ECT-R 2:
ECTR2_1818
ED133:
—
ED98:
—
HO 5096 0412:
SAEMRSA15_18620
JH1:
SaurJH1_2038
JH9:
SaurJH9_2003
JKD6008:
SAA6008_01952 (ami)
JKD6159:
SAA6159_01876 (ami)
LGA251:
—
M013:
—
MRSA252:
SAR2040
MSHR1132:
SAMSHR1132_17880
MSSA476:
SAS1869
Mu3:
SAHV_1931
Mu50:
SAV1945
MW2:
MW1886
RF122:
—
ST398:
—
T0131:
SAT0131_02079
TCH60:
HMPREF0772_11194 (amiD4)
TW20:
SATW20_19390
USA300_TCH1516:
USA300HOU_1951 (ami)
VC40:
—
⊟Genome Viewer[edit | edit source]
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.505)
N315 MKTYSEARARLRWYQGRYIDFDGWYGYQCADLAVDYIYWLLEIRMWGNAKDAINNDFKNM
NCTC8325 MKTYSEARARLRWYQGRYIDFDGWYGYQCADLAVDYIYWLLEIRMWGNAKDAINNDFKNM
Newman MKTYSEARARLRWYQGRYIDFDGWYGYQCADLAVDYIYWLLEIRMWGNAKDAINNDFKNM
USA300_FPR3757 MKTYSEARARLRWYQGRYIDFDGWYGYQCADLAVDYIYWLLEIRMWGNAKDAINNDFKNM
************************************************************
N315 ATVYENTPSFVPQIGDVAVFTKGIYKQYGHIGLVFNGGNTNQFLILEQNYDGNANTPAKL
NCTC8325 ATVYENTPSFVPQIGDVAVFTKGIYKQYGHIGLVFNGGNTNQFLILEQNYDGNANTPAKL
Newman ATVYENTPSFVPQIGDVAVFTKGIYKQYGHIGLVFNGGNTNQFLILEQNYDGNANTPAKL
USA300_FPR3757 ATVYENTPSFVPQIGDVAVFTKGIYKQYGHIGLVFNGGNTNQFLILEQNYDGNANTPAKL
************************************************************
N315 RWDNYYGCTHFIRPKYKSEGLMNKITNKINPPAQKAVGKSASKITVGSKAPYNLKWSKGA
NCTC8325 RWDNYYGCTHFIRPKYKSEGLMNKITNKVKPPAQKAVGKSASKITVGSKAPYNLKWSKGA
Newman RWDNYYGCTHFIRPKYKSEGLMNKITNKVKPPAQKAVGKSASKITVGSKAPYNLKWSKGA
USA300_FPR3757 RWDNYYGCTHFIRPKYKSEGLMNKITNKVKPPAQKAVGKSASKITVGSKAPYNLKWSKGA
****************************::******************************
N315 YFNAKIDGLGATSATRYGDNRTNYRFDVGQAVYAPGTLIYVFEIIDGWCRIYWNNHNEWI
NCTC8325 YFNAKIDGLGATSATRYGDNRTNYRFDVGQAVYAPGTLIYVFEIIDGWCRIYWNNHNEWI
Newman YFNAKIDGLGATSATRYGDNRTNYRFDVGQAVYAPGTLIYVFEIIDGWCRIYWNNHNEWI
USA300_FPR3757 YFNAKIDGLGATSATRYGDNRTNYRFDVGQAVYAPGTLIYVFEIIDGWCRIYWNNHNEWI
************************************************************
N315 WHERLIVKEAF
NCTC8325 WHERLIVKEVF
Newman WHERLIVKEVF
USA300_FPR3757 WHERLIVKEVF
*********.*
- ↑ Lorena Rodríguez-Rubio, Beatriz Martínez, Ana Rodríguez, David M Donovan, Friedrich Götz, Pilar García
The phage lytic proteins from the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 display multiple active catalytic domains and do not trigger staphylococcal resistance.
PLoS One: 2013, 8(5);e64671
[PubMed:23724076] [WorldCat.org] [DOI] (I e)Bokyung Son, Minsuk Kong, Sangryeol Ryu
The Auxiliary Role of the Amidase Domain in Cell Wall Binding and Exolytic Activity of Staphylococcal Phage Endolysins.
Viruses: 2018, 10(6);
[PubMed:29799482] [WorldCat.org] [DOI] (I e)