TARS_STAAM
ID TARS_STAAM Reviewed; 573 AA.
AC A0A0H3JPC6;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS {ECO:0000305};
DE EC=2.4.1.355 {ECO:0000269|PubMed:27973583};
DE AltName: Full=Beta-O-GlcNAc transferase {ECO:0000250|UniProtKB:A0A0H3JVA1};
DE AltName: Full=Beta-O-GlcNAc-WTA transferase {ECO:0000250|UniProtKB:A0A0H3JVA1};
DE AltName: Full=WTA glycosyltransferase {ECO:0000250|UniProtKB:A0A0H3JVA1};
DE AltName: Full=Wall teichoic acid beta-glycosyltransferase {ECO:0000303|PubMed:27973583};
GN Name=tarS {ECO:0000303|PubMed:27973583};
GN OrderedLocusNames=SAV0258 {ECO:0000312|EMBL:BAB56420.1};
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2] {ECO:0007744|PDB:5TZ8, ECO:0007744|PDB:5TZE, ECO:0007744|PDB:5TZI, ECO:0007744|PDB:5TZJ, ECO:0007744|PDB:5TZK, ECO:0007744|PDB:5U02}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-573 OF APOENZYME AND IN
RP COMPLEXES WITH SUBSTRATE AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, DOMAIN, ACTIVE
RP SITE, DRUG TARGET, AND MUTAGENESIS OF ARG-76; ASP-92; ASP-94; ASP-95;
RP GLU-178; ASP-179; ASP-198; ARG-207; HIS-211 AND SER-213.
RX PubMed=27973583; DOI=10.1371/journal.ppat.1006067;
RA Sobhanifar S., Worrall L.J., King D.T., Wasney G.A., Baumann L., Gale R.T.,
RA Nosella M., Brown E.D., Withers S.G., Strynadka N.C.;
RT "Structure and mechanism of Staphylococcus aureus TarS, the wall teichoic
RT acid beta-glycosyltransferase involved in methicillin resistance.";
RL PLoS Pathog. 12:E1006067-E1006067(2016).
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 Mediates beta-lactam resistance in methicillin resistant Staphylococcus
CC aureus (MRSA) strains. {ECO:0000269|PubMed:27973583}.
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:27973583};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:27973583};
CC Note=Can also use Mg(2+). {ECO:0000269|PubMed:27973583};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45 uM for UDP-GlcNAc {ECO:0000269|PubMed:27973583};
CC KM=1240 uM for poly(RboP) {ECO:0000269|PubMed:27973583};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000269|PubMed:27973583}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:27973583}.
CC -!- DOMAIN: Contains a trimerization domain, composed of stacked
CC carbohydrate binding modules, connected by a linker region to the
CC catalytic domain. The trimerization domain appears to be dispensable
CC for UDP-GlcNAc hydrolysis activity, but it may increase poly(RboP)
CC binding affinity. {ECO:0000269|PubMed:27973583}.
CC -!- MISCELLANEOUS: TarS is a unique target for compounds used in
CC combination with beta-lactams to treat MRSA infections.
CC {ECO:0000305|PubMed:27973583}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; BA000017; BAB56420.1; -; Genomic_DNA.
DR RefSeq; WP_000975351.1; NC_002758.2.
DR PDB; 5TZ8; X-ray; 4.00 A; A/B/C=2-573.
DR PDB; 5TZE; X-ray; 2.33 A; C/E=2-350.
DR PDB; 5TZI; X-ray; 2.30 A; C=2-350.
DR PDB; 5TZJ; X-ray; 1.90 A; A/C=2-350.
DR PDB; 5TZK; X-ray; 2.22 A; C=2-350.
DR PDB; 5U02; X-ray; 2.30 A; A=218-573.
DR PDBsum; 5TZ8; -.
DR PDBsum; 5TZE; -.
DR PDBsum; 5TZI; -.
DR PDBsum; 5TZJ; -.
DR PDBsum; 5TZK; -.
DR PDBsum; 5U02; -.
DR AlphaFoldDB; A0A0H3JPC6; -.
DR SMR; A0A0H3JPC6; -.
DR PaxDb; A0A0H3JPC6; -.
DR EnsemblBacteria; BAB56420; BAB56420; SAV0258.
DR KEGG; sav:SAV0258; -.
DR HOGENOM; CLU_018620_2_0_9; -.
DR OMA; YETESKD; -.
DR PhylomeDB; A0A0H3JPC6; -.
DR BioCyc; SAUR158878:SAV_RS01460-MON; -.
DR BRENDA; 2.4.1.355; 3352.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000002481; 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 3D-structure; 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_0000446298"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:27973583"
FT BINDING 9
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:27973583"
FT BINDING 41
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:27973583"
FT BINDING 68
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:27973583"
FT BINDING 76
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:27973583"
FT BINDING 92..94
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:27973583"
FT BINDING 94
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:27973583"
FT BINDING 127
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:27973583"
FT BINDING 178
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:27973583"
FT BINDING 207
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:27973583"
FT BINDING 211..213
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:27973583"
FT MUTAGEN 76
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27973583"
FT MUTAGEN 92
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27973583"
FT MUTAGEN 94
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27973583"
FT MUTAGEN 95
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27973583"
FT MUTAGEN 178
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27973583"
FT MUTAGEN 179
FT /note="D->N: Severe decrease in activity."
FT /evidence="ECO:0000269|PubMed:27973583"
FT MUTAGEN 198
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:27973583"
FT MUTAGEN 207
FT /note="R->A: Severe decrease in activity."
FT /evidence="ECO:0000269|PubMed:27973583"
FT MUTAGEN 211
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27973583"
FT MUTAGEN 213
FT /note="S->A: Severe decrease in activity."
FT /evidence="ECO:0000269|PubMed:27973583"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:5TZJ"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:5TZJ"
FT TURN 53..57
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:5TZJ"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 240..257
FT /evidence="ECO:0007829|PDB:5TZJ"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:5TZJ"
FT HELIX 310..322
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:5TZJ"
FT STRAND 355..363
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 365..376
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 383..392
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:5U02"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:5U02"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:5U02"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 428..438
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 469..477
FT /evidence="ECO:0007829|PDB:5U02"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 484..491
FT /evidence="ECO:0007829|PDB:5U02"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:5U02"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 506..514
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 521..527
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 530..540
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 543..550
FT /evidence="ECO:0007829|PDB:5U02"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:5U02"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:5U02"
SQ SEQUENCE 573 AA; 66257 MW; 17A9EB9064730461 CRC64;
MMKFSVIVPT YNSEKYITEL LNSLAKQDFP KTEFEVVVVD DCSTDQTLQI VEKYRNKLNL
KVSQLETNSG GPGKPRNVAL KQAEGEFVLF VDSDDYINKE TLKDAAAFID EHHSDVLLIK
MKGVNGRGVP QSMFKETAPE VTLLNSRIIY TLSPTKIYRT ALLKDNDIYF PEELKSAEDQ
LFTMKAYLNA NRISVLSDKA YYYATKREGE HMSSAYVSPE DFYEVMRLIA VEILNADLEE
AHKDQILAEF LNRHFSFSRT NGFSLKVKLE EQPQWINALG DFIQAVPERV DALVMSKLRP
LLHYARAKDI DNYRTVEESY RQGQYYRFDI VDGKLNIQFN EGEPYFEGID IAKPKVKMTA
FKFDNHKIVT ELTLNEFMIG EGHYDVRLKL HSRNKKHTMY VPLSVNANKQ YRFNIMLEDI
KAYLPKEKIW DVFLEVQIGT EVFEVRVGNQ RNKYAYTAET SALIHLNNDF YRLTPYFTKD
FNNISLYFTA ITLTDSISMK LKGKNKIILT GLDRGYVFEE GMASVVLKDD MIMGMLSQTS
ENEVEILLSK DIKKRDFKNI VKLNTAHMTY SLK
