OATWY_NEIME
ID OATWY_NEIME Reviewed; 215 AA.
AC Q93S40;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Polysialic acid O-acetyltransferase {ECO:0000303|PubMed:19525232};
DE EC=2.3.1.- {ECO:0000269|PubMed:19525232};
DE AltName: Full=Polysialyltransferase {ECO:0000303|PubMed:9439566};
DE Short=PST {ECO:0000303|PubMed:9439566};
GN Name=oatWY {ECO:0000303|PubMed:19525232};
GN Synonyms=siaD {ECO:0000303|PubMed:9439566};
OS Neisseria meningitidis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487 {ECO:0000312|EMBL:CAC38867.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serogroup Y;
RX PubMed=9439566; DOI=10.1007/pl00008618;
RA Claus H., Vogel U., Muhlenhoff M., Gerardy-Schahn R., Frosch M.;
RT "Molecular divergence of the sia locus in different serogroups of Neisseria
RT meningitidis expressing polysialic acid capsules.";
RL Mol. Gen. Genet. 257:28-34(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ACETYL-COA,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP MUTAGENESIS OF HIS-121; TRP-145 AND TYR-171.
RX PubMed=19525232; DOI=10.1074/jbc.m109.006049;
RA Lee H.J., Rakic B., Gilbert M., Wakarchuk W.W., Withers S.G.,
RA Strynadka N.C.;
RT "Structural and kinetic characterizations of the polysialic acid O-
RT acetyltransferase OatWY from Neisseria meningitidis.";
RL J. Biol. Chem. 284:24501-24511(2009).
CC -!- FUNCTION: Catalyzes the O-acetylation of capsular polymeric sialic acid
CC consisting of polymers of (2->6)-alpha-D-glucosyl-(1->4)-N-acetyl-
CC alpha-D-neuraminosyl residues. Shows high substrate specificity toward
CC polymers of sialic acid that contains a large number of residues.
CC {ECO:0000269|PubMed:19525232}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(2->6)-alpha-D-glucosyl-(1->4)-N-acetyl-alpha-D-
CC neuraminosyl](n) + n acetyl-CoA = [(2->6)-alpha-D-glucosyl-(1->4)-
CC N,7-O-diacetyl-alpha-D-neuraminosyl](n) + n CoA;
CC Xref=Rhea:RHEA:55848, Rhea:RHEA-COMP:14318, Rhea:RHEA-COMP:14319,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:139287,
CC ChEBI:CHEBI:139288; Evidence={ECO:0000269|PubMed:19525232};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(2->6)-alpha-D-glucosyl-(1->4)-N-acetyl-alpha-D-
CC neuraminosyl](n) + n acetyl-CoA = [(2->6)-alpha-D-glucosyl-(1->4)-
CC N,O(9)-diacetyl-alpha-D-neuraminosyl](n) + n CoA;
CC Xref=Rhea:RHEA:55852, Rhea:RHEA-COMP:14318, Rhea:RHEA-COMP:14320,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:139287,
CC ChEBI:CHEBI:139289; Evidence={ECO:0000269|PubMed:19525232};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=210 uM for acetyl-CoA {ECO:0000269|PubMed:19525232};
CC KM=18.5 uM for polymer of sialic acid {ECO:0000269|PubMed:19525232};
CC Note=kcat is 1.3 sec(-1) with acetyl-CoA as substrate. kcat is 2.1
CC sec(-1) with polymer of sialic acid as substrate.
CC {ECO:0000269|PubMed:19525232};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:19525232}.
CC -!- MISCELLANEOUS: Polymeric sialic acid-containing capsule provides a
CC means for the bacteria to evade the immune response during infection by
CC mimicking host sialic acid-containing cell surface structures. O-
CC acetylation of the sialic acid residues of capsular polysaccharides
CC alters their immunogenicity and susceptibility to glycosidases.
CC {ECO:0000303|PubMed:19525232}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; Y13969; CAC38867.1; -; Genomic_DNA.
DR PDB; 2WLC; X-ray; 1.95 A; A=1-215.
DR PDB; 2WLD; X-ray; 2.20 A; A/B/C=1-215.
DR PDB; 2WLE; X-ray; 2.19 A; A/B/C=1-215.
DR PDB; 2WLF; X-ray; 2.35 A; A/B/C=1-215.
DR PDB; 2WLG; X-ray; 1.90 A; A/B/C=1-215.
DR PDBsum; 2WLC; -.
DR PDBsum; 2WLD; -.
DR PDBsum; 2WLE; -.
DR PDBsum; 2WLF; -.
DR PDBsum; 2WLG; -.
DR AlphaFoldDB; Q93S40; -.
DR SMR; Q93S40; -.
DR EvolutionaryTrace; Q93S40; -.
DR GO; GO:0050208; F:polysialic-acid O-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Transferase.
FT CHAIN 1..215
FT /note="Polysialic acid O-acetyltransferase"
FT /id="PRO_0000430770"
FT BINDING 119..121
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:19525232"
FT BINDING 148
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:19525232"
FT BINDING 154
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:19525232"
FT BINDING 166
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:19525232"
FT BINDING 171..172
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:19525232"
FT BINDING 190
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:19525232"
FT MUTAGEN 121
FT /note="H->A: Reduces activity 50-fold."
FT /evidence="ECO:0000269|PubMed:19525232"
FT MUTAGEN 145
FT /note="W->A: Reduces activity 56-fold."
FT /evidence="ECO:0000269|PubMed:19525232"
FT MUTAGEN 171
FT /note="Y->A: Reduces activity 48-fold."
FT /evidence="ECO:0000269|PubMed:19525232"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2WLG"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2WLE"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2WLG"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:2WLG"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2WLG"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2WLG"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:2WLG"
SQ SEQUENCE 215 AA; 23705 MW; 27DEDA09223F1FBB CRC64;
MGTHMYSEQG INNTINISTT SLTNATQLTV IGNNNSVYIG NNCKIVSSNI RLKGNNITLF
IADDVENMGL VCSLHSDCSL QIQAKTTMGN GEITIAEKGK ISIGKDCMLA HGYEIRNTDM
HPIYSLENGE RINHGKDVII GNHVWLGRNV TILKGVCIPN NVVVGSHTVL YKSFKEPNCV
IAGSPAKIVK ENIVWGRKMY HSTMYDDPTL NEFYK
