TARP_STAAN
ID TARP_STAAN Reviewed; 327 AA.
AC A0A0H3JNB0;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarP {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:30464342};
DE AltName: Full=WTA glycosyltransferase {ECO:0000303|PubMed:30464342};
GN Name=tarP {ECO:0000303|PubMed:30464342};
GN OrderedLocusNames=SA1808 {ECO:0000312|EMBL:BAB43088.1};
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
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:6H1J, ECO:0007744|PDB:6H21, ECO:0007744|PDB:6H2N, ECO:0007744|PDB:6H4F, ECO:0007744|PDB:6H4M, ECO:0007744|PDB:6HNQ}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP SUBSTRATE; SUBSTRATE ANALOGS AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, PATHWAY, SUBUNIT, DISRUPTION PHENOTYPE, DRUG TARGET, ACTIVE SITE,
RP AND MUTAGENESIS OF ARG-76; ASP-92; ASP-94; TYR-152; GLU-180; ASP-181;
RP ASP-209; LYS-255; ARG-259; ARG-262; HIS-263 AND ILE-322.
RC STRAIN=N315;
RX PubMed=30464342; DOI=10.1038/s41586-018-0730-x;
RA Gerlach D., Guo Y., De Castro C., Kim S.H., Schlatterer K., Xu F.F.,
RA Pereira C., Seeberger P.H., Ali S., Codee J., Sirisarn W., Schulte B.,
RA Wolz C., Larsen J., Molinaro A., Lee B.L., Xia G., Stehle T., Peschel A.;
RT "Methicillin-resistant Staphylococcus aureus alters cell wall glycosylation
RT to evade immunity.";
RL Nature 563:705-709(2018).
CC -!- FUNCTION: Attaches beta-O-GlcNAc (beta-O-N-acetyl-D-glucosamine)
CC residues to the C3 position of poly(RboP)-wall teichoic acids (WTAs).
CC Attenuates immunogenicity of WTA and protects S.aureus against
CC adaptative host defenses by allowing bacteria to evade recognition by
CC preexisting anti-S.aureus antibodies. Also protects the cell from
CC podophage infection. {ECO:0000269|PubMed:30464342}.
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-([3-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:58948,
CC Rhea:RHEA-COMP:12840, Rhea:RHEA-COMP:15259, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:133896,
CC ChEBI:CHEBI:142885; Evidence={ECO:0000269|PubMed:30464342};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:30464342};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000269|PubMed:30464342}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:30464342}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to a substantially
CC increased capacity of human neutrophils to phagocytose opsonized
CC S.aureus. Inactivation renders the cell susceptible to podophages.
CC {ECO:0000269|PubMed:30464342}.
CC -!- MISCELLANEOUS: TarP inhibitors could be used as a new strategy for
CC rendering methicillin resistant Staphylococcus aureus (MRSA) strains
CC susceptible to human host defenses. {ECO:0000305|PubMed:30464342}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; BA000018; BAB43088.1; -; Genomic_DNA.
DR RefSeq; WP_001558608.1; NC_002745.2.
DR PDB; 6H1J; X-ray; 1.86 A; A/B/C=1-327.
DR PDB; 6H21; X-ray; 1.80 A; A/B/C=1-327.
DR PDB; 6H2N; X-ray; 1.95 A; A/B/C=1-327.
DR PDB; 6H4F; X-ray; 2.18 A; A/B/C/D/E/F/G/H/I/O/P/Q=1-327.
DR PDB; 6H4M; X-ray; 2.73 A; A/B/C/D/E/F/G/H/I/O/P/Q=1-327.
DR PDB; 6HNQ; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/O/P/Q=1-327.
DR PDBsum; 6H1J; -.
DR PDBsum; 6H21; -.
DR PDBsum; 6H2N; -.
DR PDBsum; 6H4F; -.
DR PDBsum; 6H4M; -.
DR PDBsum; 6HNQ; -.
DR AlphaFoldDB; A0A0H3JNB0; -.
DR SMR; A0A0H3JNB0; -.
DR EnsemblBacteria; BAB43088; BAB43088; BAB43088.
DR KEGG; sau:SA1808; -.
DR HOGENOM; CLU_025996_7_0_9; -.
DR OMA; CIYIKEN; -.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000000751; 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: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 Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Manganese; Metal-binding; Teichoic acid biosynthesis; Transferase;
KW Virulence.
FT CHAIN 1..327
FT /note="Poly(ribitol-phosphate) beta-N-
FT acetylglucosaminyltransferase TarP"
FT /id="PRO_0000446443"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:30464342"
FT BINDING 9
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:30464342"
FT BINDING 41
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:30464342"
FT BINDING 68
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:30464342"
FT BINDING 76
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:30464342"
FT BINDING 92..94
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:30464342"
FT BINDING 94
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 76
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 92
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 94
FT /note="D->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 152
FT /note="Y->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 180
FT /note="E->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 181
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 209
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 255
FT /note="K->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 259
FT /note="R->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 262
FT /note="R->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 263
FT /note="H->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT MUTAGEN 322
FT /note="I->E: Increase in activity."
FT /evidence="ECO:0000269|PubMed:30464342"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6H21"
FT TURN 145..149
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 224..238
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 246..263
FT /evidence="ECO:0007829|PDB:6H21"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:6H21"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 306..313
FT /evidence="ECO:0007829|PDB:6H21"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:6H21"
SQ SEQUENCE 327 AA; 37812 MW; CB258B0C4780F6DF CRC64;
MKKVSVIMPT FNNGEKLHRT ISSVLNQTMK STDYELIIID DHSNDNGETL NVIKKYKGLV
RFKQLKKNSG NASVPRNTGL KMSKAEYVFF LDSDDLLHER ALEDLYNYGK ENNSDLIIGK
YGVEGKGRSV PKAIFEKGNV AKADIIDNSI FYALSVLKMF KKSVIDKNKI KFKTFSKTAE
DQLFTIEFLM NSKNYSIKTD YEYYIVVNDF ESSNHLSVNK STGNQYFATI NEIYKAIYKS
PIYKNQEKRH QLAGKYTTRL LRHGQKKNFA NSKMKYEDKI EWLNNFSKTI NKVPRDSDKY
VTQIFNLKLE AIRQNDLLAV MIADKLL
