ID   PSEH_CAMJJ              Reviewed;         157 AA.
AC   A1W0U7; Q2M5R3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Acetyltransferase PseH;
DE            EC=2.3.1.-;
DE   AltName: Full=Pseudaminic acid biosynthesis protein H;
GN   Name=pseH; OrderedLocusNames=CJJ81176_1330;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=81-176;
RX   PubMed=11461915; DOI=10.1074/jbc.m104529200;
RA   Thibault P., Logan S.M., Kelly J.F., Brisson J.-R., Ewing C.P., Trust T.J.,
RA   Guerry P.;
RT   "Identification of the carbohydrate moieties and glycosylation motifs in
RT   Campylobacter jejuni flagellin.";
RL   J. Biol. Chem. 276:34862-34870(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION.
RC   STRAIN=81-176;
RX   PubMed=16684771; DOI=10.1074/jbc.m603777200;
RA   McNally D.J., Hui J.P., Aubry A.J., Mui K.K., Guerry P., Brisson J.R.,
RA   Logan S.M., Soo E.C.;
RT   "Functional characterization of the flagellar glycosylation locus in
RT   Campylobacter jejuni 81-176 using a focused metabolomics approach.";
RL   J. Biol. Chem. 281:18489-18498(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC69289.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY102622; ABC69289.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000538; EAQ72810.1; -; Genomic_DNA.
DR   RefSeq; WP_002781802.1; NC_008787.1.
DR   AlphaFoldDB; A1W0U7; -.
DR   SMR; A1W0U7; -.
DR   STRING; 354242.CJJ81176_1330; -.
DR   EnsemblBacteria; EAQ72810; EAQ72810; CJJ81176_1330.
DR   GeneID; 66543716; -.
DR   KEGG; cjj:CJJ81176_1330; -.
DR   eggNOG; COG1670; Bacteria.
DR   HOGENOM; CLU_013985_20_1_7; -.
DR   OMA; NHYELEG; -.
DR   Proteomes; UP000000646; 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; Transferase.
FT   CHAIN           1..157
FT                   /note="Acetyltransferase PseH"
FT                   /id="PRO_0000418963"
FT   DOMAIN          5..152
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ   SEQUENCE   157 AA;  18816 MW;  B4E1356905CF1B8B CRC64;
     MIKLKNFTEL NSQEIELIFK WRNHPDINQF MKTKYIDFEE HLRFLKKLHQ DSSKKYFLVF
     QDEQIIGVID FVNITTKSCE FGLYAKPNLK GVGQILMNEI IKYAFENLKV NTLKAYVFKD
     NRKALKLYQQ NHFTIYDEDK DFYHICLKQS DCKALPS