Jump to navigation
Jump to search
⊟Summary[edit | edit source]
- pan ID?: SAUPAN001132000
- symbol?: tarF
- synonym:
- description?: CDP-glycerol--glycerophosphate glycerophosphotransferase
- CDP-glycerol--glycerophosphate glycerophosphotransferase
- CDP-glycerol glycerophosphotransferase family protein
- putative teichoic acid biosynthesis protein F
- TagF domain-containing protein
- teichoic acid biosynthesis protein F
- teichoic acid biosynthesis protein F, putative
- teichoic acid glycerol-phosphate transferase TarF
- CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase
- cdp-glycerol:poly(glycerophosphate) glycerophosphotransFerase (polyglycerol phosphate polymerase) (cgptase) (majorteichoic acid biosynthesis protein f)
- CDP-glycerol:poly domain protein
- CDP-glycerol glycerophosphotransferase
- CDP-ribitol:poly(ribitol phosphate) ribitol phosphotransferase
- glycerophosphotransferase, TarF
- Poly(glycerophosphate) glycerophosphotransferase family protein
- TagF domain protein
- trancated TagF
descriptions from strain specific annotations:
- strand?: +
- coordinates?: 1401281..1402514
- synteny block?: BlockID0006520
- occurrence?: in 100% of 34 strains
tarF : CDP-glycerol:glycerophosphate glycerophosphotransferase [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_0254
08BA02176:
C248_0242
11819-97:
MS7_0244
6850:
RSAU_000198 (tagF)
71193:
ST398NM01_0267
ECT-R 2:
ECTR2_215
ED133:
SAOV_0193
ED98:
SAAV_0222
HO 5096 0412:
SAEMRSA15_02130
JH1:
SaurJH1_0245
JH9:
SaurJH9_0239
JKD6008:
SAA6008_00228 (tarF)
JKD6159:
SAA6159_00231 (tarF)
JSNZ:
JSNZ_000194 (tarF)
LGA251:
SARLGA251_02180 (tarF)
M013:
M013TW_0235
MRSA252:
SAR0251
MSHR1132:
SAMSHR1132_02220
MSSA476:
SAS0231
Mu3:
SAHV_0253
Mu50:
SAV0254
MW2:
MW0230
RF122:
SAB0193
ST398:
SAPIG0267
T0131:
SAT0131_00247
TCH60:
HMPREF0772_10248 (tagF)
TW20:
SATW20_02560 (tarF)
USA300_TCH1516:
USA300HOU_0265 (tagF)
VC40:
SAVC_01010
⊟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 MIKNTIKKLIEHSIYTTFKLLSKLPNKNLIYFESFHGKQYSDNPKALYEYLTEHSDAQLI
N315 MIKNTIKKLIEHSIYTTFKLLSKLPNKNLIYFESFHGKQYSDNPKALYEYLTEHSDAQLI
NCTC8325 MIKNTIKKLIEHSIYTTFKLLSKLPNKNLIYFESFHGKQYSDNPKALYEYLTEHSDAQLI
Newman MIKNTIKKLIEHSIYTTFKLLSKLPNKNLIYFESFHGKQYSDNPKALYEYLTEHSDAQLI
USA300_FPR3757 MIKNTIKKLIEHSIYTTFKLLSKLPNKNLIYFESFHGKQYSDNPKALYEYLTEHSDAQLI
************************************************************
COL WGVKKGYEHIFQQHNVPYVTKFSMKWFLAMPRAKAWMINTRTPDWLYKSPRTTYLQTWHG
N315 WGVKKGYEHIFQQYNVPYVTKFSMKWFLAMPRAKAWMINTRTPDWLYKSPRTTYLQTWHG
NCTC8325 WGVKKGYEHIFQQHNVPYVTKFSMKWFLAMPRAKAWMINTRTPDWLYKSPRTTYLQTWHG
Newman WGVKKGYEHIFQQHNVPYVTKFSMKWFLAMPRAKAWMINTRTPDWLYKSPRTTYLQTWHG
USA300_FPR3757 WGVKKGYEHIFQQHNVPYVTKFSMKWFLAMPRAKAWMINTRTPDWLYKSPRTTYLQTWHG
*************:**********************************************
COL TPLKKIGLDISNVKMLGTNTQNYQDGFKKESQRWDYLVSPNPYSTSIFQNAFHVSRDKIL
N315 TPLKKIGLDISNVKMLGTNTQNYQDGFKKESQRWDYLVSPNPYSTSIFQHAFHVSRDKIL
NCTC8325 TPLKKIGLDISNVKMLGTNTQNYQDGFKKESQRWDYLVSPNPYSTSIFQNAFHVSRDKIL
Newman TPLKKIGLDISNVKMLGTNTQNYQDGFKKESQRWDYLVSPNPYSTSIFQNAFHVSRDKIL
USA300_FPR3757 TPLKKIGLDISNVKMLGTNTQNYQDGFKKESQRWDYLVSPNPYSTSIFQNAFHVSRDKIL
*************************************************:**********
COL ETGYPRNDKLSHKRNDTEYINGIKTRLNIPLDKKVIMYAPTWRDDEAIREGSYQFNVNFD
N315 ETGYPRNDKLSHKRNDTEYINGIKTRLNIPLDKKVIMYAPTWRDDEAIREGSYQFNVNFD
NCTC8325 ETGYPRNDKLSHKRNDTEYINGIKTRLNIPLDKKVIMYAPTWRDDEAIREGSYQFNVNFD
Newman ETGYPRNDKLSHKRNDTEYINGIKTRLNIPLDKKVIMYAPTWRDDEAIREGSYQFNVNFD
USA300_FPR3757 ETGYPRNDKLSHKRNDTEYINGIKTRLNIPLDKKVIMYAPTWRDDEAIREGSYQFNVNFD
************************************************************
COL IEALRQALDDDYVILLRMHYLVVTRIDEHDDFVKDVSDYEDISDLYLISDALVTDYSSVM
N315 IEALRQALDDDYVILLRMHYLVVTRIDEHDDFVKDVSDYEDISDLYLISDALVTDYSSVM
NCTC8325 IEALRQALDDDYVILLRMHYLVVTRIDEHDDFVKDVSDYEDISDLYLISDALVTDYSSVM
Newman IEALRQALDDDYVILLRMHYLVVTRIDEHDDFVKDVSDYEDISDLYLISDALVTDYSSVM
USA300_FPR3757 IEALRQALDDDYVILLRMHYLVVTRIDEHDDFVKDVSDYEDISDLYLISDALVTDYSSVM
************************************************************
COL FDFGVLKRPQIFYAYDLDKYGDELRGFYMDYKKELPGPIVENQTALIDALKQIDETANEY
N315 FDFGVLKRPQIFYAYDLDKYGDELRGFYMDYKKELPGPIVENQTALIDALKQIDETANEY
NCTC8325 FDFGVLKRPQIFYAYDLDKYGDELRGFYMDYKKELPGPIVENQTALIDALKQIDETANEY
Newman FDFGVLKRPQIFYAYDLDKYGDELRGFYMDYKKELPGPIIENQTALIDALKQIDETANEY
USA300_FPR3757 FDFGVLKRPQIFYAYDLDKYGDELRGFYMDYKKELPGPIVENQTALIDALKQIDETANEY
***************************************:********************
COL IEARTVFYQKFCSLEDGQASQRICQTIFK
N315 IEARTVFYQKFCSLEDGQASQRICQTIFK
NCTC8325 IEARTVFYQKFCSLEDGQASQRICQTIFK
Newman IEARTVFYQKFCSLEDGQASQRICQTIFK
USA300_FPR3757 IEARTVFYQKFCSLEDGQASQRICQTIFK
*****************************
- ↑ 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)