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⊟Summary[edit | edit source]
- pan ID?: SAUPAN001123000
- symbol?: tarI'
- synonym:
- description?: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase 1 (4-diphosphocytidyl-2C-methyl-D-erythritol synthase 1)(MEP cytidylyltransferase 1) (MCT 1)
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase 1, IspD_1
- 4-diphosphocytidyl-2C-methyl-D-erythritol synthase, putative
- D-ribitol-5-phosphate cytidylyltransferase
- ribitol-5-phosphate cytidylyltransferase
descriptions from strain specific annotations:
- strand?: +
- coordinates?: 1396608..1397338
- synteny block?: BlockID0006430
- occurrence?: in 100% of 34 strains
tarI12 (tarI') : ribitol-5-phosphate cytidylyltransferase 2 [1]
- Wall teichoic acid biosynthesis in Staphylococcus aureus is complicated by the presence of multiple overlapping pathways that are at least situationally functionally redundant. Initial steps involve modification of undecaprenyl phosphate with GlcNAc (TarO) and ManNAc (TarA) and then priming with two equivalents of glycerophosphate (TarB, TarF). This makes a starter unit for two types of WTA:
- TarL can prime and polymerize approximately 40 units of ribitol phosphate resulting into extended-length teichoic acids. The CDP-ribitol substrate is generated by the TarI1 and TarJ1 enzymes
- TarK can prime and polymerize approximately 20 units of ribitol phosphate resulting into short-length teichoic acids. The CDP-ribitol substrate is generated by the TarI2 and TarJ2 enzymes
- TarJ encodes ribulose-5-phosphate reductase (alt. ribitol-5-phosphate dehydrogenase) which reduces ribulose phosphate to ribitol phosphate
- TarI encodes ribitol-5-phosphate cytidylyltransferase which activates ribitol as CDP-ribitol
⊟Orthologs[edit | edit source]
04-02981:
SA2981_0251
08BA02176:
C248_0238
11819-97:
MS7_0239 (ispD1)
6850:
RSAU_000195
71193:
ST398NM01_0263
ECT-R 2:
ECTR2_212
ED133:
SAOV_0190
ED98:
SAAV_0219 (ispD)
HO 5096 0412:
SAEMRSA15_02100
JH1:
SaurJH1_0242
JH9:
SaurJH9_0236
JKD6008:
SAA6008_00224 (ispD_1)
JKD6159:
SAA6159_00228 (ispD_1)
JSNZ:
JSNZ_000191
LGA251:
SARLGA251_02150 (ispD1)
M013:
M013TW_0232
MRSA252:
SAR0246 (ispD)
MSHR1132:
SAMSHR1132_02190
MSSA476:
SAS0227 (ispD)
Mu3:
SAHV_0250
Mu50:
SAV0251 (ispD)
MW2:
MW0227 (ispD)
RF122:
SAB0190
ST398:
SAPIG0263
T0131:
SAT0131_00243
TCH60:
HMPREF0772_10252 (ispD1)
TW20:
SATW20_02530 (ispD1)
USA300_TCH1516:
USA300HOU_0262 (ispD2)
VC40:
SAVC_00995
⊟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 MIYAGILAGGIGSRMGNVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISH
N315 MIYAGILAGGIGSRMGNVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISH
NCTC8325 --------------MGNVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISH
Newman MIYAGILAGGIGSRMGNVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISH
USA300_FPR3757 --------------MGNVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISH
**********************************************
COL TQDILKKYNITDQRVKVVAGGTDRNETIMNIIDHIRNVNGINNDDVIVTHDAVRPFLTQR
N315 TQDILKKYNITDQRVKVVAGGTDRNETIMNIIDHIRNVNGINNDDVIVTHDAVRPFLTQR
NCTC8325 TQDILKKYNITDQRVKVVAGGTDRNETIMNIIDHIRNVNGINNDDVIVTHDAVRPFLTQR
Newman TQDILKKYNITDQRVKVVAGGTDRNETIMNIIDHIRNVNGINNDDVIVTHDAVRPFLTQR
USA300_FPR3757 TQDILKKYNITDQRVKVVAGGTDRNETIMNIIDHIRNVNGINNDDVIVTHDAVRPFLTQR
************************************************************
COL IIKENIEVAAKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQGQTPQSFNIKLLQDS
N315 IIKENIEVAAKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQGQTPQSFNIKLLQDS
NCTC8325 IIKENIEVAAKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQGQTPQSFNIKLLQDS
Newman IIKENIEVAAKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQGQTPQSFNIKLLQDS
USA300_FPR3757 IIKENIEVAAKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQGQTPQSFNIKLLQDS
************************************************************
COL YRALSSEQKEILSDACKIIVESGHAVKLVRGELYNIKVTTPYDLKVANAIIQGDIADD
N315 YRALSSEQKEILSDACKIIVESGHAVKLVRGELYNIKVTTPYDLKVANAIIQGDIADD
NCTC8325 YRALSSEQKEILSDACKIIVESGHAVKLVRGELYNIKVTTPYDLKVANAIIQGDIADD
Newman YRALSSEQKEILSDACKIIVESGHAVKLVRGELYNIKVTTPYDLKVANAIIQGDIADD
USA300_FPR3757 YRALSSEQKEILSDACKIIVESGHAVKLVRGELYNIKVTTPYDLKVANAIIQGDIADD
**********************************************************
- ↑ Mark P Pereira, Michael A D'Elia, Justyna Troczynska, Eric D Brown
Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus leads to functionally redundant poly(ribitol phosphate) polymerases.
J Bacteriol: 2008, 190(16);5642-9
[PubMed:18556787] [WorldCat.org] [DOI] (I p)Ziliang Qian, Yanbin Yin, Yong Zhang, Lingyi Lu, Yixue Li, Ying Jiang
Genomic characterization of ribitol teichoic acid synthesis in Staphylococcus aureus: genes, genomic organization and gene duplication.
BMC Genomics: 2006, 7;74
[PubMed:16595020] [WorldCat.org] [DOI] (I e)Jonathan G Swoboda, Jennifer Campbell, Timothy C Meredith, Suzanne Walker
Wall teichoic acid function, biosynthesis, and inhibition.
Chembiochem: 2010, 11(1);35-45
[PubMed:19899094] [WorldCat.org] [DOI] (I p)