TARM_STAAC
ID TARM_STAAC Reviewed; 493 AA.
AC A0A0H2WWV6; A0A0J9X256; A0A0J9X257;
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) alpha-N-acetylglucosaminyltransferase {ECO:0000305};
DE EC=2.4.1.70 {ECO:0000269|PubMed:20185825, ECO:0000269|PubMed:25624472, ECO:0000269|PubMed:25697358};
DE AltName: Full=WTA GlcNAc-transferase {ECO:0000303|PubMed:20185825};
GN Name=tarM {ECO:0000303|PubMed:20185825};
GN OrderedLocusNames=SACOL1043 {ECO:0000312|EMBL:AAW36508.1};
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 487-TRP--SER-493.
RC STRAIN=COL, and RN4220;
RX PubMed=20185825; DOI=10.1074/jbc.m109.096172;
RA Xia G., Maier L., Sanchez-Carballo P., Li M., Otto M., Holst O.,
RA Peschel A.;
RT "Glycosylation of wall teichoic acid in Staphylococcus aureus by TarM.";
RL J. Biol. Chem. 285:13405-13415(2010).
RN [3] {ECO:0007744|PDB:4X6L, ECO:0007744|PDB:4X7M, ECO:0007744|PDB:4X7P, ECO:0007744|PDB:4X7R}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEXES WITH UDP AND UDP-GLCNAC
RP AND OF MUTANT ARG-117 IN COMPLEX WITH UDP AND ACCEPTOR SUBSTRATE ANALOG,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MUTAGENESIS OF HIS-249; ARG-326; LYS-331; GLU-403 AND GLU-411.
RC STRAIN=subsp. aureus 21178;
RX PubMed=25624472; DOI=10.1073/pnas.1418084112;
RA Sobhanifar S., Worrall L.J., Gruninger R.J., Wasney G.A., Blaukopf M.,
RA Baumann L., Lameignere E., Solomonson M., Brown E.D., Withers S.G.,
RA Strynadka N.C.;
RT "Structure and mechanism of Staphylococcus aureus TarM, the wall teichoic
RT acid alpha-glycosyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E576-E585(2015).
RN [4] {ECO:0007744|PDB:4WAC, ECO:0007744|PDB:4WAD}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, AND MUTAGENESIS
RP OF LYS-136; ASN-138; ASN-180; HIS-249; ARG-326; LYS-331; GLU-403 AND
RP GLU-411.
RX PubMed=25697358; DOI=10.1074/jbc.m114.619924;
RA Koc C., Gerlach D., Beck S., Peschel A., Xia G., Stehle T.;
RT "Structural and enzymatic analysis of TarM glycosyltransferase from
RT Staphylococcus aureus reveals an oligomeric protein specific for the
RT glycosylation of wall teichoic acid.";
RL J. Biol. Chem. 290:9874-9885(2015).
CC -!- FUNCTION: Attaches N-acetyl-alpha-D-glucosamine residues to poly(RboP)-
CC wall teichoic acids (WTAs). {ECO:0000269|PubMed:20185825,
CC ECO:0000269|PubMed:25624472, ECO:0000269|PubMed:25697358}.
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-alpha-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:21012,
CC Rhea:RHEA-COMP:12840, Rhea:RHEA-COMP:14256, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:133896,
CC ChEBI:CHEBI:139145; EC=2.4.1.70;
CC Evidence={ECO:0000269|PubMed:20185825, ECO:0000269|PubMed:25624472,
CC ECO:0000269|PubMed:25697358};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=65 uM for UDP-GlcNAc {ECO:0000269|PubMed:25624472};
CC KM=390 uM for WTA {ECO:0000269|PubMed:25624472};
CC Note=kcat is 126 min(-1). {ECO:0000269|PubMed:25624472};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000269|PubMed:20185825}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:25624472,
CC ECO:0000269|PubMed:25697358}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:20185825}.
CC -!- DOMAIN: Assembles into a propeller-like homotrimer in which each blade
CC contains a GT-B-type glycosyltransferase domain with a typical Rossmann
CC fold. Assembles into a trimer using a novel trimerization domain,
CC termed the HUB domain. {ECO:0000269|PubMed:25697358}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene leads to resistance to
CC serogroup B phages. Disruption leads to altered WTA that lacks the
CC alpha-GlcNAc residues. Mutant exhibits no major changes in growth
CC kinetics, microscopic appearance or antibiotic susceptibility.
CC {ECO:0000269|PubMed:20185825}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000305}.
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DR EMBL; CP000046; AAW36508.1; -; Genomic_DNA.
DR RefSeq; WP_000719184.1; NC_002951.2.
DR PDB; 4WAC; X-ray; 2.40 A; A=1-493.
DR PDB; 4WAD; X-ray; 2.80 A; A=1-493.
DR PDB; 4X6L; X-ray; 3.19 A; A/B/C/D=1-493.
DR PDB; 4X7M; X-ray; 2.40 A; A/B=1-493.
DR PDB; 4X7P; X-ray; 3.40 A; A/B=1-493.
DR PDB; 4X7R; X-ray; 2.15 A; A/B=1-493.
DR PDBsum; 4WAC; -.
DR PDBsum; 4WAD; -.
DR PDBsum; 4X6L; -.
DR PDBsum; 4X7M; -.
DR PDBsum; 4X7P; -.
DR PDBsum; 4X7R; -.
DR AlphaFoldDB; A0A0H2WWV6; -.
DR SMR; A0A0H2WWV6; -.
DR EnsemblBacteria; AAW36508; AAW36508; SACOL1043.
DR KEGG; sac:SACOL1043; -.
DR PATRIC; fig|904724.3.peg.2374; -.
DR HOGENOM; CLU_009583_21_4_9; -.
DR OMA; FFITEEQ; -.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000000530; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047269; F:poly(ribitol-phosphate) N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR001296; Glyco_trans_1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Cytoplasm;
KW Glycosyltransferase; Teichoic acid biosynthesis; Transferase.
FT CHAIN 1..493
FT /note="Poly(ribitol-phosphate) alpha-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000446297"
FT BINDING 17
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:25624472,
FT ECO:0000269|PubMed:25697358"
FT BINDING 59
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:25624472"
FT BINDING 249
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:25697358"
FT BINDING 326
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:25624472"
FT BINDING 331
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:25624472"
FT BINDING 383
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:25624472,
FT ECO:0000269|PubMed:25697358"
FT BINDING 403..411
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:25624472,
FT ECO:0000269|PubMed:25697358"
FT MUTAGEN 117
FT /note="G->R: Forms monomers. No change in activity."
FT /evidence="ECO:0000269|PubMed:25624472"
FT MUTAGEN 136
FT /note="K->S: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:25697358"
FT MUTAGEN 138
FT /note="N->Q: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:25697358"
FT MUTAGEN 180
FT /note="N->W: No change in activity."
FT /evidence="ECO:0000269|PubMed:25697358"
FT MUTAGEN 249
FT /note="H->A: Severe decrease in activity."
FT /evidence="ECO:0000269|PubMed:25624472,
FT ECO:0000269|PubMed:25697358"
FT MUTAGEN 326
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25624472"
FT MUTAGEN 326
FT /note="R->S: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:25697358"
FT MUTAGEN 331
FT /note="K->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25624472,
FT ECO:0000269|PubMed:25697358"
FT MUTAGEN 403
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25624472,
FT ECO:0000269|PubMed:25697358"
FT MUTAGEN 411
FT /note="E->A: Severe decrease in activity."
FT /evidence="ECO:0000269|PubMed:25624472,
FT ECO:0000269|PubMed:25697358"
FT MUTAGEN 487..493
FT /note="Missing: In 52B2; loss of activity. Phage-resistant
FT phenotype."
FT /evidence="ECO:0000269|PubMed:20185825"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 17..31
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:4X7R"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:4X7R"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:4X7R"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:4X7R"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 333..346
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:4X7R"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:4X7R"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:4X7R"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 446..457
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 460..477
FT /evidence="ECO:0007829|PDB:4X7R"
FT HELIX 480..492
FT /evidence="ECO:0007829|PDB:4X7R"
SQ SEQUENCE 493 AA; 57275 MW; 74625BDEF25678F0 CRC64;
MKKIFMMVHE LDVNKGGMTS SMFNRSKEFY DADIPADIVT FDYKGNYDEI IKALKKQGKM
DRRTKMYNVF EYFKQISNNK HFKSNKLLYK HISERLKNTI EIEESKGISR YFDITTGTYI
AYIRKSKSEK VIDFFKDNKR IERFSFIDNK VHMKETFNVD NKVCYQVFYD EKGYPYISRN
INANNGAVGK TYVLVNKKEF KNNLALCVYY LEKLIKDSKD SIMICDGPGS FPKMFNTNHK
NAQKYGVIHV NHHENFDDTG AFKKSEKYII ENANKINGVI VLTEAQRLDI LNQFDVENIF
TISNFVKIHN APKHFQTEKI VGHISRMVPT KRIDLLIEVA ELVVKKDNAV KFHIYGEGSV
KDKIAKMIED KNLERNVFLK GYTTTPQKCL EDFKLVVSTS QYEGQGLSMI EAMISKRPVV
AFDIKYGPSD FIEDNKNGYL IENHNINDMA DKILQLVNND VLAAEFGSKA RENIIEKYST
ESILEKWLNL FNS
