NEUO_ECOK1
ID NEUO_ECOK1 Reviewed; 307 AA.
AC A1ADJ6; Q4A3R7; Q58WP5;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Polysialic acid O-acetyltransferase {ECO:0000303|PubMed:15809431, ECO:0000303|PubMed:17519228};
DE EC=2.3.1.136 {ECO:0000269|PubMed:15809431, ECO:0000269|PubMed:17519228};
DE AltName: Full=Capsule O-acetyl transferase {ECO:0000312|EMBL:CAH65463.1};
GN Name=neuO {ECO:0000303|PubMed:15809431, ECO:0000303|PubMed:17519228};
GN ORFNames=APECO1_4217 {ECO:0000312|EMBL:ABJ01736.1};
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=RS164 {ECO:0000312|EMBL:AAX11174.1};
RX PubMed=15809431; DOI=10.1073/pnas.0407428102;
RA Deszo E.L., Steenbergen S.M., Freedberg D.I., Vimr E.R.;
RT "Escherichia coli K1 polysialic acid O-acetyltransferase gene, neuO, and
RT the mechanism of capsule form variation involving a mobile contingency
RT locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5564-5569(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF HIS-210 AND
RP TRP-234.
RX PubMed=17519228; DOI=10.1074/jbc.m703044200;
RA Bergfeld A.K., Claus H., Vogel U., Muhlenhoff M.;
RT "Biochemical characterization of the polysialic acid-specific O-
RT acetyltransferase NeuO of Escherichia coli K1.";
RL J. Biol. Chem. 282:22217-22227(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 66-307, AND SUBUNIT.
RX PubMed=21390252; DOI=10.1371/journal.pone.0017403;
RA Schulz E.C., Bergfeld A.K., Ficner R., Muehlenhoff M.;
RT "Crystal structure analysis of the polysialic acid specific O-
RT acetyltransferase NeuO.";
RL PLoS ONE 6:E17403-E17403(2011).
CC -!- FUNCTION: Catalyzes the O-acetylation of capsular polymeric sialic
CC acid. Shows high substrate specificity toward polymers of sialic acid
CC that contains a large number of residues. {ECO:0000269|PubMed:15809431,
CC ECO:0000269|PubMed:17519228}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(2->8)-N-acetyl-alpha-D-neuraminosyl](n) + n acetyl-CoA =
CC [(2->8)-N,O(9)-diacetyl-alpha-D-neuraminosyl](n) + n CoA;
CC Xref=Rhea:RHEA:11608, Rhea:RHEA-COMP:14315, Rhea:RHEA-COMP:14317,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:139252,
CC ChEBI:CHEBI:139286; EC=2.3.1.136;
CC Evidence={ECO:0000269|PubMed:15809431, ECO:0000269|PubMed:17519228};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(2->8)-N-acetyl-alpha-D-neuraminosyl](n) + n acetyl-CoA =
CC [(2->8)-O(7),N-diacetyl-alpha-D-neuraminosyl](n) + n CoA;
CC Xref=Rhea:RHEA:11604, Rhea:RHEA-COMP:14315, Rhea:RHEA-COMP:14316,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:139252,
CC ChEBI:CHEBI:139285; EC=2.3.1.136;
CC Evidence={ECO:0000269|PubMed:15809431, ECO:0000269|PubMed:17519228};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for acetyl-CoA {ECO:0000269|PubMed:17519228};
CC KM=1.17 mM for polymer of sialic acid {ECO:0000269|PubMed:17519228};
CC Note=kcat is 0.51 sec(-1) with acetyl-CoA as substrate. kcat is 1.99
CC sec(-1) with polymer of sialic acid as substrate.
CC {ECO:0000269|PubMed:17519228};
CC -!- SUBUNIT: Homotrimer (PubMed:21390252). Hexamer formed by two
CC homotrimers (PubMed:17519228). {ECO:0000269|PubMed:21390252,
CC ECO:0000303|PubMed:17519228}.
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:15809431, ECO:0000303|PubMed:17519228}.
CC -!- MISCELLANEOUS: The catalytic efficiency increases linearly with the
CC number of RLKTQDS repeats. {ECO:0000269|PubMed:15809431,
CC ECO:0000269|PubMed:17519228}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; AY779018; AAX11174.1; -; Genomic_DNA.
DR EMBL; AJ851330; CAH65463.1; -; Genomic_DNA.
DR EMBL; CP000468; ABJ01736.1; -; Genomic_DNA.
DR PDB; 3JQY; X-ray; 1.70 A; A/B/C=66-307.
DR PDBsum; 3JQY; -.
DR AlphaFoldDB; A1ADJ6; -.
DR SMR; A1ADJ6; -.
DR EnsemblBacteria; ABJ01736; ABJ01736; APECO1_4217.
DR KEGG; ecv:APECO1_4217; -.
DR HOGENOM; CLU_051638_6_0_6; -.
DR BRENDA; 2.3.1.136; 2026.
DR Proteomes; UP000008216; Chromosome.
DR GO; GO:0050208; F:polysialic-acid O-acetyltransferase activity; IDA:UniProtKB.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Repeat; Transferase.
FT CHAIN 1..307
FT /note="Polysialic acid O-acetyltransferase"
FT /id="PRO_0000430771"
FT REPEAT 3..9
FT /note="1"
FT REPEAT 10..16
FT /note="2"
FT REPEAT 17..23
FT /note="3"
FT REPEAT 24..30
FT /note="4"
FT REPEAT 31..37
FT /note="5"
FT REPEAT 38..44
FT /note="6"
FT REPEAT 45..51
FT /note="7"
FT REPEAT 52..58
FT /note="8"
FT REPEAT 59..65
FT /note="9"
FT REPEAT 66..72
FT /note="10"
FT REPEAT 73..79
FT /note="11"
FT REPEAT 80..86
FT /note="12"
FT REPEAT 87..93
FT /note="13"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3..93
FT /note="13 X 7 AA tandem repeat of RLKTQDS encoded by a 7
FT nucleotide repeat"
FT COMPBIAS 1..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208..210
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q93S40"
FT BINDING 237
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q93S40"
FT BINDING 243
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q93S40"
FT BINDING 261
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q93S40"
FT BINDING 278
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q93S40"
FT MUTAGEN 210
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17519228"
FT MUTAGEN 234
FT /note="W->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17519228"
FT CONFLICT 4..24
FT /note="Missing (in Ref. 1; AAX11174)"
FT CONFLICT 4..10
FT /note="Missing (in Ref. 2; CAH65463)"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 114..124
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 134..146
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3JQY"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:3JQY"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:3JQY"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:3JQY"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3JQY"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:3JQY"
SQ SEQUENCE 307 AA; 34518 MW; 42F2D7884D8C1656 CRC64;
MLRLKTQDSR LKTQDSRLKT QDSRLKTQDS RLKTQDSRLK TQDSRLKTQD SRLKTQDSRL
KTQDSRLKTQ DSRLKTQDSR LKTQDSRLKT QDSFSVDDNG SGNVFVCGDL VNSKENKVQF
NGNNNKLIIE DDVECRWLTV IFRGDNNYVR IHKNSKIKGD IVATKGSKVI IGRRTTIGAG
FEVVTDKCNV TIGHDCMIAR DVILRASDGH PIFDIHSKKR INWAKDIIIS SYVWVGRNVS
IMKGVSVGSG SVIGYGSIVT KDVPSMCAAA GNPAKIIKRN IIWARTDKAE LISDDKRCSS
YHAKLTQ
