ID   PSEH_CAMJE              Reviewed;         157 AA.
AC   Q0P8U4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Acetyltransferase PseH;
DE            EC=2.3.1.-;
DE   AltName: Full=Pseudaminic acid biosynthesis protein H;
GN   Name=pseH; OrderedLocusNames=Cj1313;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: Catalyzes the third step in the biosynthesis of pseudaminic
CC       acid, a sialic-acid-like sugar that is used to modify flagellin.
CC       Mediates N-4 acetylation of UDP-4-amino-4,6-dideoxy-beta-L-AltNAc to
CC       form UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; AL111168; CAL35427.1; -; Genomic_DNA.
DR   PIR; F81274; F81274.
DR   RefSeq; WP_002858467.1; NC_002163.1.
DR   RefSeq; YP_002344703.1; NC_002163.1.
DR   AlphaFoldDB; Q0P8U4; -.
DR   SMR; Q0P8U4; -.
DR   IntAct; Q0P8U4; 17.
DR   STRING; 192222.Cj1313; -.
DR   PaxDb; Q0P8U4; -.
DR   PRIDE; Q0P8U4; -.
DR   DNASU; 905605; -.
DR   EnsemblBacteria; CAL35427; CAL35427; Cj1313.
DR   GeneID; 905605; -.
DR   KEGG; cje:Cj1313; -.
DR   PATRIC; fig|192222.6.peg.1295; -.
DR   eggNOG; COG1670; Bacteria.
DR   HOGENOM; CLU_013985_20_1_7; -.
DR   OMA; NHYELEG; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR020036; PseH.
DR   Pfam; PF13302; Acetyltransf_3; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR03585; PseH; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..157
FT                   /note="Acetyltransferase PseH"
FT                   /id="PRO_0000418962"
FT   DOMAIN          5..152
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   157 AA;  18775 MW;  5438B202B4BEDC67 CRC64;
     MIKLKNFAEL NSQEIKLIFK WRNHPDISQF MKTKHIDFEE HLRFIRNLHQ DSNKKYFLVF
     QDEQIIGVID FVNITTKSCE FGLYAIPDLK GVGQVLMNEI KKYAFEILKV DTLKAYVFKD
     NHKALKLYQQ NHFTIYDEDK DFYYVCLKQS HCKALPS