ID   PSEF_CAMJE              Reviewed;         232 AA.
AC   Q0P8U6;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Pseudaminic acid cytidylyltransferase;
DE            EC=2.7.7.81;
DE   AltName: Full=Pseudaminic acid biosynthesis protein F;
GN   Name=pseF; OrderedLocusNames=Cj1311;
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 final step in the biosynthesis of pseudaminic
CC       acid, a sialic-acid-like sugar that is used to modify flagellin.
CC       Mediates the activation of pseudaminic acid with CMP by forming CMP-
CC       pseudaminic acid (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + pseudaminate = CMP-pseudaminate + diphosphate;
CC         Xref=Rhea:RHEA:32083, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:63282, ChEBI:CHEBI:63680; EC=2.7.7.81;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
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DR   EMBL; AL111168; CAL35425.1; -; Genomic_DNA.
DR   PIR; D81274; D81274.
DR   RefSeq; WP_002777693.1; NC_002163.1.
DR   RefSeq; YP_002344701.1; NC_002163.1.
DR   AlphaFoldDB; Q0P8U6; -.
DR   SMR; Q0P8U6; -.
DR   IntAct; Q0P8U6; 41.
DR   STRING; 192222.Cj1311; -.
DR   PaxDb; Q0P8U6; -.
DR   PRIDE; Q0P8U6; -.
DR   EnsemblBacteria; CAL35425; CAL35425; Cj1311.
DR   GeneID; 905603; -.
DR   KEGG; cje:Cj1311; -.
DR   PATRIC; fig|192222.6.peg.1293; -.
DR   eggNOG; COG1083; Bacteria.
DR   HOGENOM; CLU_042930_1_0_7; -.
DR   OMA; AYHMKEL; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR020039; PseF.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03584; PseF; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..232
FT                   /note="Pseudaminic acid cytidylyltransferase"
FT                   /id="PRO_0000418937"
SQ   SEQUENCE   232 AA;  26627 MW;  7C151EC3223DC9B1 CRC64;
     MKNLCIIPAR GGSKRIPRKN IIDFLGKPLI SYSIENALNS GIFDEVVLSS DDEEIIEVAL
     KYGAKAPFVR DKNLSDDYAS STAVVQNAIE ILQSQNQIYD HVCCLYATAP LLNKDILKQA
     YEKFIQNQSK FLFAATEFEY PIQRAFYLNE NNQVYMFDEK HYKSRSQDLT KAYHDAGAFY
     FGTSKAWLEE DFIFKPHSSV FVLPRNLVCD IDTIQDLEFA KILYKVNHES AF