ID   HASA_STRP3              Reviewed;         419 AA.
AC   P0DB60; Q877W4; Q8K5G6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Hyaluronan synthase;
DE            EC=2.4.1.212;
DE   AltName: Full=Hyaluronate synthase;
DE   AltName: Full=Hyaluronic acid synthase;
DE            Short=HA synthase;
GN   Name=hasA; OrderedLocusNames=SpyM3_1851;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
CC   -!- FUNCTION: Glycosaminoglycan synthesis. The hyaluronic acid capsule is
CC       involved in the pathogenicity of group A Streptococci; it may be the
CC       major virulence determinant (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-
CC         acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP;
CC         Xref=Rhea:RHEA:20465, Rhea:RHEA-COMP:12583, Rhea:RHEA-COMP:12585,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP-
CC         alpha-D-glucuronate = [hyaluronan](n+1) + H(+) + UDP;
CC         Xref=Rhea:RHEA:12528, Rhea:RHEA-COMP:12585, Rhea:RHEA-COMP:12587,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NodC/HAS family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-25 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AE014074; AAM80458.1; -; Genomic_DNA.
DR   PIR; A48755; A48755.
DR   RefSeq; WP_011055113.1; NC_004070.1.
DR   AlphaFoldDB; P0DB60; -.
DR   SMR; P0DB60; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; AAM80458; AAM80458; SpyM3_1851.
DR   KEGG; spg:SpyM3_1851; -.
DR   HOGENOM; CLU_029695_4_0_9; -.
DR   OMA; DVIVPCF; -.
DR   UniPathway; UPA00341; -.
DR   Proteomes; UP000000564; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050501; F:hyaluronan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030213; P:hyaluronan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Cell membrane; Glycosyltransferase;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..419
FT                   /note="Hyaluronan synthase"
FT                   /id="PRO_0000197166"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   419 AA;  47842 MW;  040D4EF5756C582F CRC64;
     MPIFKKTLIV LSFICLISIL IYLNMYLFGT STVGIYGVIL ITYLVIKLGL SFLYEPFKGN
     PHDYKVAAVI PSYNEDAESL LETLKSVLAQ TYPLSEIYIV DDGSSNTDAI QLIEEYVNRE
     VDICRNVIVH RSLVNKGKRH AQAWAFERSD ADVFLTVDSD TYIYPNALEE LLKSFNDETV
     YAATGHLNAR NRQTNLLTRL TDIRYDNAFG VERAAQSLTG NILVCSGPLS IYRREVIIPN
     LERYKNQTFL GLPVSIGDDR CLTNYAIDLG RTVYQSTARC DTDVPFQLKS YLKQQNRWNK
     SFFRESIISV KKILSNPIVA LWTIFEVVMF MMLIVAIGNL LFNQAIQLDL IKLFAFLSII
     FIVALCRNVH YMVKHPASFL LSPLYGILHL FVLQPLKLYS LCTIKNTEWG TRKKVTIFK