TARS_STAAW
ID TARS_STAAW Reviewed; 573 AA.
AC A0A0H3JVA1;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS {ECO:0000305};
DE EC=2.4.1.355 {ECO:0000269|PubMed:23027967};
DE AltName: Full=Beta-O-GlcNAc transferase {ECO:0000303|PubMed:23027967};
DE AltName: Full=Beta-O-GlcNAc-WTA transferase {ECO:0000303|PubMed:23027967};
DE AltName: Full=WTA glycosyltransferase {ECO:0000303|PubMed:23027967};
GN Name=tarS {ECO:0000303|PubMed:23027967};
GN OrderedLocusNames=MW0234 {ECO:0000312|EMBL:BAB94099.1};
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INDUCTION, DISRUPTION PHENOTYPE, AND
RP DRUG TARGET.
RC STRAIN=MW2, and RN4220;
RX PubMed=23027967; DOI=10.1073/pnas.1209126109;
RA Brown S., Xia G., Luhachack L.G., Campbell J., Meredith T.C., Chen C.,
RA Winstel V., Gekeler C., Irazoqui J.E., Peschel A., Walker S.;
RT "Methicillin resistance in Staphylococcus aureus requires glycosylated wall
RT teichoic acids.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18909-18914(2012).
CC -!- FUNCTION: Attaches beta-O-GlcNAc (beta-O-N-acetyl-D-glucosamine)
CC residues to the C4 position of poly(RboP)-wall teichoic acids (WTAs).
CC Prefers UDP-GlcNAc as a donor substrate and is specific for
CC poly(ribitol phosphate) WTAs. Can also use UDP-Glc and UDP-GalNAc, but
CC not UDP-galactose or UDP-glucuronic acid. Mediates beta-lactam
CC resistance in methicillin resistant Staphylococcus aureus (MRSA)
CC strains. {ECO:0000269|PubMed:23027967}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-[(D-ribitylphospho)(n)-di{(2R)-glycerylphospho}]-N-acetyl-
CC beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-
CC trans,octa-cis-undecaprenyl diphosphate + n UDP-N-acetyl-alpha-D-
CC glucosamine = 4-O-([2-N-acetyl-beta-D-glucosaminyl-1-D-
CC ribitylphospho](n)-di{[2R]-1-glycerylphospho})-N-acetyl-beta-D-
CC mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-
CC undecaprenyl diphosphate + n H(+) + n UDP; Xref=Rhea:RHEA:55672,
CC Rhea:RHEA-COMP:12840, Rhea:RHEA-COMP:14257, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:133896,
CC ChEBI:CHEBI:139146; EC=2.4.1.355;
CC Evidence={ECO:0000269|PubMed:23027967};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A0H3JPC6};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000269|PubMed:23027967}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:A0A0H3JPC6}.
CC -!- INDUCTION: Expression is up-regulated in the presence of beta-lactams.
CC {ECO:0000269|PubMed:23027967}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant has no growth or cell division
CC defects, but mutant shows increased susceptibility to beta-lactams.
CC Deletion of the gene leads to the production of only alpha-O-
CC GlcNAcylated WTAs. {ECO:0000269|PubMed:23027967}.
CC -!- MISCELLANEOUS: TarS is a unique target for compounds used in
CC combination with beta-lactams to treat MRSA infections.
CC {ECO:0000305|PubMed:23027967}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; BA000033; BAB94099.1; -; Genomic_DNA.
DR RefSeq; WP_000975365.1; NC_003923.1.
DR AlphaFoldDB; A0A0H3JVA1; -.
DR SMR; A0A0H3JVA1; -.
DR EnsemblBacteria; BAB94099; BAB94099; BAB94099.
DR KEGG; sam:MW0234; -.
DR HOGENOM; CLU_018620_2_0_9; -.
DR OMA; YETESKD; -.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000000418; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR041038; TarS_C1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF18674; TarS_C1; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Manganese; Metal-binding; Teichoic acid biosynthesis;
KW Transferase; Virulence.
FT CHAIN 1..573
FT /note="Poly(ribitol-phosphate) beta-N-
FT acetylglucosaminyltransferase TarS"
FT /id="PRO_0000446299"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JPC6"
FT BINDING 9
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JPC6"
FT BINDING 41
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JPC6"
FT BINDING 68
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JPC6"
FT BINDING 76
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JPC6"
FT BINDING 92..94
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JPC6"
FT BINDING 94
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JPC6"
FT BINDING 127
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JPC6"
FT BINDING 178
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JPC6"
FT BINDING 207
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JPC6"
FT BINDING 211..213
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3JPC6"
SQ SEQUENCE 573 AA; 66255 MW; 45A3FB79484316E8 CRC64;
MMKFSVIVPT YNSEKYITEL LNSLAKQDFP KTEFEVVVVD DCSTDQTLQI VEKYRNKLNL
KVSQLETNSG GPGKPRNVAL KQAEGEFVLF VDSDDYINKE TLKDAAAFID EHHSDVLLIK
MKGVNGRGVP QSMFKETAPE VTLLNSRIIY TLSPTKIYRT TLLKDNDIYF PEELKSAEDQ
LFTMKAYLNA NRISVLSDKA YYYATKREGE HMSSAYVSPE DFYEVMRLIA VEILNADLEE
AHKDQILAEF LNRHFSFSRT NGFSLKVKLE DQPQWINALG DFIQAVPERV DALVMSKLRP
LLHYARAKDI DNYRTVEESY RQGQYYRFDI VDGKLNIQFN EGEPYFEGID IAKPKVKMTA
FKFDNHKIVT ELTLNEFMIG EGHYDVRLKL HSRNKKHTMY VPLSVNANKQ YRFNIMLEDI
KAYLPKEKIW DVFLEVQIGT EVFEVRVGNQ RNKYAYTAET SALIHLNNDF YRLTPYFTKD
FNNISLYFTA ITLTDSISLK LKGKNKIILT GLDRGYVFEE GMASVVLKDD MIMGMLSQTS
ENEVEILLSK DIKKRDFKNI VKLNTAHMTY SLK
