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⊟Summary[edit | edit source]
- pan ID?: SAUPAN001858000
- symbol?: sirTM
- synonym:
- description?: deacetylase SIR2
- deacetylase SIR2
- NAD-dependent deacetylase
- NAD-dependent protein deacetylase, SIR2 family
- NAD-dependent protein deacetylase of SIR2family
- NAD-dependent protein deacetylase SIR2 family-like protein
- Sir2 family NAD-dependent protein deacetylase-like protein
- SIR2 family protein
- Sir2 silent information regulator family NAD-dependent deacetylase
descriptions from strain specific annotations:
- strand?: +
- coordinates?: 2355841..2356801
- synteny block?: BlockID0012330
- occurrence?: in 94% of 34 strains
sirTM (srtN) : ADP ribosyltransferase SIR2 [1]
SirTM proteins are structurally related to sirtuin deacetylases but rather than deacetylating target proteins, SirTM adds an ADP-ribose. This posttranslational modification appears to be exclusive to lipoylated proteins like GcvH-L where it protects from redox stress responses. It might also prevent association between co-regulated oxidoreductases (OfrB, SAUPAN001855000, SAUPAN001862000) and GcvH-L where the ribosylate-free lipoylate moiety of GcvH-L can power the ROS-scavenging oxidoreductase activity. SirTM enzymes work with a partner macrodomain (SirHR) protein that recognizes "MARylated" (mono-ADP-ribosylated) lipoylproteins and performs the ADP ribose removal function.
⊟Orthologs[edit | edit source]
04-02981:
SA2981_0325
08BA02176:
—
11819-97:
MS7_0316
6850:
RSAU_000272
71193:
ST398NM01_0406
ECT-R 2:
ECTR2_286
ED133:
SAOV_0352
ED98:
SAAV_0294
HO 5096 0412:
SAEMRSA15_02820
JH1:
SaurJH1_0385
JH9:
SaurJH9_0375
JKD6008:
SAA6008_00303
JKD6159:
SAA6159_00302
JSNZ:
JSNZ_000281
LGA251:
SARLGA251_02880
M013:
M013TW_0307
MRSA252:
SAR0323
MSHR1132:
SAMSHR1132_03000
MSSA476:
SAS0303
Mu3:
SAHV_0323
Mu50:
SAV0326
MW2:
MW0303
RF122:
SAB0276
ST398:
—
T0131:
SAT0131_00331 (valS)
TCH60:
HMPREF0772_10169
TW20:
SATW20_03940
USA300_TCH1516:
USA300HOU_0347
VC40:
SAVC_01380
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL -MQSSKWNAMSLLMDDKTKQAEVLRTAIDEADAIVIGIGAGMSASDGFTYVGERFTENFP
N315 MMQSSKWNAMSLLMDEKTKQAEVLRTAIDEADAIVIGIGAGMSASDGFTYVGERFTENFP
NCTC8325 -MQSSKWNAMSLLMDDKTKQAEVLRTAIDEADAIVIGIGAGMSASDGFTYVGERFTENFP
Newman -MQSSKWNAMSLLMDDKTKQAEVLRTAIDEADAIVIGIGAGMSASDGFTYVGERFTENFP
USA300_FPR3757 -MQSSKWNAMSLLMDDKTKQAEVLRTAIDEADAIVIGIGAGMSASDGFTYVGERFTENFP
**************:********************************************
COL DFIEKYRFFDMLQASLHPYGSWQEYWAFESRFITLNYLDQPVGQSYLALKSLVEGKQYHI
N315 DFIEKYRFFDMLQASLHPYGSWQEYWAFESRFITLNYLDQPVGQSYLALKSLVEGKQYHI
NCTC8325 DFIEKYRFFDMLQASLHPYGSWQEYWAFESRFITLNYLDQPVGQSYLALKSLVEGKQYHI
Newman DFIEKYRFFDMLQASLHPYGSWQEYWAFESRFITLNYLDQPVGQSYLALKSLVEGKQYHI
USA300_FPR3757 DFIEKYRFFDMLQASLHPYGSWQEYWAFESRFITLNYLDQPVGQSYLALKSLVEGKQYHI
************************************************************
COL ITTNADNAFDVADYDMTHVFHIQGEYILQQCSQHCHAQTYRNDDLIRKMVVAQQDMLIPW
N315 ITTNADNAFDAAEYDMTHVFHIQGEYILQQCSQHCHAQTYRNDDLIRKMVVAQQDMLIPW
NCTC8325 ITTNADNAFDVADYDMTHVFHIQGEYILQQCSQHCHAQTYRNDDLIRKMVVAQQDMLIPW
Newman ITTNADNAFDVADYDMTHVFHIQGEYILQQCSQHCHAQTYRNDDLIRKMVVAQQDMLIPW
USA300_FPR3757 ITTNADNAFDVADYDMTHVFHIQGEYILQQCSQHCHAQTYRNDDLIRKMVVAQQDMLIPW
**********.*:***********************************************
COL EMIPRCPKCDAPMEVNKRKAEVGMVEDAEFHAQLHRYNAFLEQHQDDKVLYLEIGIGYTT
N315 EMIPRCPKCDAPMEVNKRKAEVGMVEDAEFHAQLQRYNAFLEQHQDDKVLYLEIGIGYTT
NCTC8325 EMIPRCPKCDAPMEVNKRKAEVGMVEDAEFHAQLHRYNAFLEQHQDDKVLYLEIGIGYTT
Newman EMIPRCPKCDAPMEVNKRKAEVGMVEDAEFHAQLHRYNAFLEQHQDDKVLYLEIGIGYTT
USA300_FPR3757 EMIPRCPKCDAPMEVNKRKAEVGMVEDAEFHAQLHRYNAFLEQHQDDKVLYLEIGIGYTT
**********************************:*************************
COL PQFVKHPFQRMTRKNENALYMTMNKKAYRIPNSIQERTIHLTEDISTLITAALRNDSTTK
N315 PQFVKHPFQRMTRKNENAIYMTMNKKAYRIPNSIQERTIHLTEDISTLITTALRNDSTTQ
NCTC8325 PQFVKHPFQRMTRKNENALYMTMNKKAYRIPNSIQERTIHLTEDISTLITAALRNDSTTK
Newman PQFVKHPFQRMTRKNENALYMTMNKKAYRIPNSIQERTIHLTEDISTLITAALRNDSTTK
USA300_FPR3757 PQFVKHPFQRMTRKNENALYMTMNKKAYRIPNSIQERTIHLTEDISTLITAALRNDSTTK
******************:*******************************:********:
COL NNNIGETEDVLNRTD
N315 NNNIGETEDVLNRTD
NCTC8325 NNNIGETEDVLNRTD
Newman NNNIGETEDVLNRTD
USA300_FPR3757 NNNIGETEDVLNRTD
***************
- ↑ Johannes Gregor Matthias Rack, Rosa Morra, Eva Barkauskaite, Rolf Kraehenbuehl, Antonio Ariza, Yue Qu, Mary Ortmayer, Orsolya Leidecker, David R Cameron, Ivan Matic, Anton Y Peleg, David Leys, Ana Traven, Ivan Ahel
Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens.
Mol Cell: 2015, 59(2);309-20
[PubMed:26166706] [WorldCat.org] [DOI] (I p)Rachel M Burckhardt, Brandi A Buckner, Jorge C Escalante-Semerena
Staphylococcus aureus modulates the activity of acetyl-Coenzyme A synthetase (Acs) by sirtuin-dependent reversible lysine acetylation.
Mol Microbiol: 2019, 112(2);588-604
[PubMed:31099918] [WorldCat.org] [DOI] (I p)Antonio Ariza, Qiang Liu, Nathan P Cowieson, Ivan Ahel, Dmitri V Filippov, Johannes Gregor Matthias Rack
Evolutionary and molecular basis of ADP-ribosylation reversal by zinc-dependent macrodomains.
J Biol Chem: 2024, 300(10);107770
[PubMed:39270823] [WorldCat.org] [DOI] (I p)