ID   NEUAH_CAMJE             Reviewed;         235 AA.
AC   Q0P8S7;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=CMP-N,N'-diacetyllegionaminic acid synthase;
DE            EC=2.7.7.82;
GN   Name=legF; Synonyms=ptmB; OrderedLocusNames=Cj1331;
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).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND NOMENCLATURE.
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=19282391; DOI=10.1093/glycob/cwp039;
RA   Schoenhofen I.C., Vinogradov E., Whitfield D.M., Brisson J.R., Logan S.M.;
RT   "The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving
RT   novel GDP-linked precursors.";
RL   Glycobiology 19:715-725(2009).
CC   -!- FUNCTION: Involved in biosynthesis of legionaminic acid (5,7-diamino-
CC       3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a
CC       sialic acid-like derivative that is incorporated into flagellin via O-
CC       linkage to Ser/Thr. Catalyzes the conversion of N,N'-
CC       diacetyllegionaminic acid (Leg5Ac7Ac) and CTP into CMP-N,N'-
CC       diacetyllegionaminic acid (CMP-Leg5Ac7Ac).
CC       {ECO:0000269|PubMed:19282391}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CTP + N,N-diacetyllegionaminate = CMP-N,N-
CC         diacetyllegionaminate + diphosphate; Xref=Rhea:RHEA:34675,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:68669,
CC         ChEBI:CHEBI:68670; EC=2.7.7.82;
CC         Evidence={ECO:0000269|PubMed:19282391};
CC   -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
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DR   EMBL; AL111168; CAL35444.1; -; Genomic_DNA.
DR   PIR; H81276; H81276.
DR   RefSeq; WP_002864263.1; NC_002163.1.
DR   RefSeq; YP_002344720.1; NC_002163.1.
DR   AlphaFoldDB; Q0P8S7; -.
DR   SMR; Q0P8S7; -.
DR   IntAct; Q0P8S7; 7.
DR   STRING; 192222.Cj1331; -.
DR   PaxDb; Q0P8S7; -.
DR   PRIDE; Q0P8S7; -.
DR   EnsemblBacteria; CAL35444; CAL35444; Cj1331.
DR   GeneID; 905623; -.
DR   KEGG; cje:Cj1331; -.
DR   PATRIC; fig|192222.6.peg.1313; -.
DR   eggNOG; COG1083; Bacteria.
DR   HOGENOM; CLU_042930_1_0_7; -.
DR   OMA; NCDEMES; -.
DR   BioCyc; MetaCyc:MON-16354; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Bacterial flagellum biogenesis; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..235
FT                   /note="CMP-N,N'-diacetyllegionaminic acid synthase"
FT                   /id="PRO_0000424187"
SQ   SEQUENCE   235 AA;  26661 MW;  AF0E63913FBCFD99 CRC64;
     MAEILCTICA RGGSKGVKNK NIRKINKLEM IAYSIIQAQN SKLFKHIVIS TDSDEIASVA
     QKYGAEVFFK REAHLANDRT AKLPVMRDAL LRSEEHFKTC FETLIDLDAS APLRSSLDIK
     KAYESFVEND NSNLITAVPA RRNPYFNLVE IQNNKVVKSK EGNFTTRQSA PKCYDMNASI
     YIFKRDYLLE NDSVFGKNTG LFVMDESTAF DIDSELDFKI VEFLISLKNL SPKDF