ID   NEUA_STRA3              Reviewed;         413 AA.
AC   P0A4V0; Q53598; Q9S0S5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=N-acylneuraminate cytidylyltransferase;
DE            EC=2.7.7.43;
DE   AltName: Full=CMP-N-acetylneuraminic acid synthase;
DE            Short=CMP-NeuNAc synthase;
DE   AltName: Full=CMP-sialic acid synthase;
GN   Name=neuA; OrderedLocusNames=gbs1233;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=COH31 / Serotype III;
RX   PubMed=8830246; DOI=10.1046/j.1365-2958.1996.395931.x;
RA   Haft R.F., Wessels M.R., Mebane M.F., Conaty N., Rubens C.E.;
RT   "Characterization of cpsF and its product CMP-N-acetylneuraminic acid
RT   synthetase, a group B streptococcal enzyme that can function in K1 capsular
RT   polysaccharide biosynthesis in Escherichia coli.";
RL   Mol. Microbiol. 19:555-563(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=COH1 / Serotype III;
RX   PubMed=10913080; DOI=10.1128/jb.182.16.4466-4477.2000;
RA   Chaffin D.O., Beres S.B., Yim H.H., Rubens C.E.;
RT   "The serotype of type Ia and III group B streptococci is determined by the
RT   polymerase gene within the polycistronic capsule operon.";
RL   J. Bacteriol. 182:4466-4477(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
CC   -!- FUNCTION: Catalyzes the formation of CMP-N-acetylneuraminic acid (CMP-
CC       NeuNAc), which is essential for the formation of the capsule.
CC       {ECO:0000269|PubMed:8830246}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylneuraminate + CTP = a CMP-N-acyl-beta-neuraminate +
CC         diphosphate; Xref=Rhea:RHEA:11344, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:60073, ChEBI:CHEBI:68671; EC=2.7.7.43;
CC         Evidence={ECO:0000269|PubMed:8830246};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CMP-NeuNAc synthase family. {ECO:0000305}.
CC   -!- CAUTION: Was originally called CpsF. {ECO:0000305|PubMed:8830246}.
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DR   EMBL; U19899; AAB50271.1; -; Genomic_DNA.
DR   EMBL; AF163833; AAD53077.1; -; Genomic_DNA.
DR   EMBL; AL766849; CAD46892.1; -; Genomic_DNA.
DR   RefSeq; WP_000802346.1; NC_004368.1.
DR   AlphaFoldDB; P0A4V0; -.
DR   SMR; P0A4V0; -.
DR   STRING; 211110.gbs1233; -.
DR   EnsemblBacteria; CAD46892; CAD46892; CAD46892.
DR   KEGG; san:neuA; -.
DR   eggNOG; COG1083; Bacteria.
DR   eggNOG; COG2755; Bacteria.
DR   HOGENOM; CLU_660110_0_0_9; -.
DR   OMA; LQWITEI; -.
DR   Proteomes; UP000000823; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR003329; Cytidylyl_trans.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF02348; CTP_transf_3; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Capsule biogenesis/degradation; Cytoplasm; Exopolysaccharide synthesis;
KW   Magnesium; Manganese; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..413
FT                   /note="N-acylneuraminate cytidylyltransferase"
FT                   /id="PRO_0000213208"
FT   CONFLICT        392..413
FT                   /note="TQEANDLLQSQYQLFVDEVKTL -> DSRG (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   413 AA;  47670 MW;  9089CD673ABD1FC8 CRC64;
     MKPICIIPAR SGSKGLPDKN MLFLAGKPMI FHTIDAAIES GMFDKKDIFV STDSELYREI
     CLERGISVVM RKPELSTDQA TSYDMLKDFL SDYEDNQEFV LLQVTSPLRK SWHIKEAMEY
     YSSHDVDNVV SFSEVEKHPG LFTTLSDKGY AIDMVGADKG YRRQDLQPLY YPNGAIFISN
     KETYLREKSF FTSRTYAYQM AKEFSLDVDT RDDFIHVIGH LFFDYAIREK ENKVFYKEGY
     SRLFNREASK IILGDSKTIS ISLENYHNYS QGGVTLATML ENLPNFLTAN VTEAFVSIGV
     NDLITGYSVE EIFSNFQKLY SLLAENKIKM RFTTIAYTLF RETVNNADIE KINQWLTEFC
     YQNQIPLLDI NRFLSKDGNL NYHLTSDGLH FTQEANDLLQ SQYQLFVDEV KTL