ID   NEUA_STRA1              Reviewed;         413 AA.
AC   P0A4V1; Q3K0U2; Q53598; Q9S0S5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=SAK_1247;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=OI1 / Serotype Ia;
RX   PubMed=10464185; DOI=10.1128/jb.181.17.5176-5184.1999;
RA   Yamamoto S., Miyake K., Koike Y., Watanabe M., Machida Y., Ohta M.,
RA   Iijima S.;
RT   "Molecular characterization of type-specific capsular polysaccharide
RT   biosynthesis genes of Streptococcus agalactiae type Ia.";
RL   J. Bacteriol. 181:5176-5184(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA   Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA   Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA   Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA   Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA   Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA   Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA   Wessels M.R., Rappuoli R., Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
CC   -!- FUNCTION: Catalyzes the formation of CMP-N-acetylneuraminic acid (CMP-
CC       NeuNAc), which is essential for the formation of the capsule.
CC       {ECO:0000250}.
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   -!- 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}.
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DR   EMBL; AB028896; BAA82290.1; -; Genomic_DNA.
DR   EMBL; CP000114; ABA45253.1; -; Genomic_DNA.
DR   PIR; S70912; S70912.
DR   RefSeq; WP_000802346.1; NC_007432.1.
DR   AlphaFoldDB; P0A4V1; -.
DR   SMR; P0A4V1; -.
DR   KEGG; sak:SAK_1247; -.
DR   HOGENOM; CLU_660110_0_0_9; -.
DR   OMA; LQWITEI; -.
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   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Cytoplasm; Exopolysaccharide synthesis;
KW   Magnesium; Manganese; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..413
FT                   /note="N-acylneuraminate cytidylyltransferase"
FT                   /id="PRO_0000213207"
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