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⊟Summary[edit | edit source]
- pan ID?: SAUPAN001124000
- symbol?: tarJ'
- synonym:
- description?: alcohol dehydrogenase
- alcohol dehydrogenase
- alcohol dehydrogenase catalytic domain-containing protein
- alcohol dehydrogenase, zinc-containing
- alcohol dehydrogenase, zinc-containing, putative
- putative alcohol dehydrogenase
- ribitol-5-phosphate dehydrogenase
- zinc-containing alcohol dehydrogenase
- Ribitol-5-phosphate 2-dehydrogenase
- xylitol dehydrogenase
- alcohol dehydrogenase GroES-like domain protein
- pseudogene
- putative ribitol-5-phosphate dehydrogenase (Ribulose-5-P reductase)
- putative zinc-binding dehydrogenase
- zinc-binding dehydrogenase family protein
descriptions from strain specific annotations:
- strand?: +
- coordinates?: 1397304..1398357
- synteny block?: BlockID0006440
- occurrence?: in 100% of 34 strains
tarJ2 (tarJ') : ribulose-5-phosphate reductase 2 [1]
• A crystal structure is available : 6XHK
- 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_0252
08BA02176:
C248_0239
11819-97:
MS7_0240
6850:
RSAU_000196
71193:
ST398NM01_0264
ECT-R 2:
ECTR2_213
ED133:
SAOV_0191
ED98:
SAAV_0220
HO 5096 0412:
SAEMRSA15_02110
JH1:
SaurJH1_0243
JH9:
SaurJH9_0237
JKD6008:
SAA6008_00225
JKD6159:
SAA6159_00229
JSNZ:
JSNZ_000192
LGA251:
SARLGA251_02160 (tarJ')
M013:
M013TW_0233
MRSA252:
SAR0247
MSHR1132:
SAMSHR1132_02200
MSSA476:
SAS0228
Mu3:
SAHV_0251
Mu50:
SAV0252
MW2:
MW0228
RF122:
SAB0191
ST398:
SAPIG0264
T0131:
SAT0131_00244
TCH60:
HMPREF0772_10251 (tarJ2)
TW20:
SATW20_02540 (tarJ')
USA300_TCH1516:
USA300HOU_0263
VC40:
SAVC_01000
⊟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 MINQVYQLVAPRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYTGRRDENVLRKKLPM
N315 MINQVYQLVAPRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYTGRRDENVLRKKLPM
NCTC8325 MINQVYQLVAPRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYTGRRDENVLRKKLPM
Newman MINQVYQLVAPRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYTGRRDENVLRKKLPM
USA300_FPR3757 MINQVYQLVAPRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYTGRRDENVLRKKLPM
************************************************************
COL SLVHEAVGEVVFDSKGVFEKGTKVVMVPNTPTEQHHIIAENYLASSYFRSSGYDGFMQDY
N315 SLVHEAVGEVVFDSKGVFEKGTKVVMVPNTPTEQHHIIAENYLASSYFRSSGYDGFMQDY
NCTC8325 SLVHEAVGEVVFDSKGVFEKGTKVVMVPNTPTEQHHIIAENYLASSYFRSSGYDGFMQDY
Newman SLVHEAVGEVVFDSKGVFEKGTKVVMVPNTPTEQHHIIAENYLASSYFRSSGYDGFMQDY
USA300_FPR3757 SLVHEAVGEVVFDSKGVFEKGTKVVMVPNTPTEQHHIIAENYLASSYFRSSGYDGFMQDY
************************************************************
COL VVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKSIPLKTSFGIWGDGNLGYITA
N315 VVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKSIPLKNSFGIWGDGNLGYITA
NCTC8325 VVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKSIPLKTSFGIWGDGNLGYITA
Newman VVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKSIPLKTSFGIWGDGNLGYITA
USA300_FPR3757 VVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKSIPLKTSFGIWGDGNLGYITA
********************************************.***************
COL ILLRKLYPEAKTYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKIDHAFECVGGKGSQVALQ
N315 ILLRKLYPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKIDHAFECVGGKGSQVALQ
NCTC8325 ILLRKLYPEAKTYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKIDHAFECVGGKGSQVALQ
Newman ILLRKLYPEAKTYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKIDHAFECVGGKGSQVALQ
USA300_FPR3757 ILLRKLYPEAKTYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKIDHAFECVGGKGSQVALQ
*********** ************************************************
COL QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDI
N315 QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDI
NCTC8325 QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDI
Newman QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDI
USA300_FPR3757 QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDI
************************************************************
COL VEKLALLKGHEINVCTMQDIVQAFEMDLSTSWGKTVLKWTI
N315 VEKLALLKGHEINVCTMQDIVQAFEMDLSTSWGKTVLKWTI
NCTC8325 VEKLALLKGHEINVCTMQDIVQAFEMDLSTSWGKTVLKWTI
Newman VEKLALLKGHEINVCTMQDIVQAFEMDLSTSWGKTVLKWTI
USA300_FPR3757 VEKLALLKGHEINVCTMQDIVQAFEMDLSTSWGKTVLKWTI
*****************************************
- ↑ 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)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)