ID   HASA_STRPY              Reviewed;         419 AA.
AC   P0C0H0; Q08494; Q54865; Q54868;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 68.
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;
OS   Streptococcus pyogenes.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WF50;
RX   PubMed=8276791; DOI=10.1016/s0021-9258(17)42330-1;
RA   Dougherty B.A., van de Rijn I.;
RT   "Molecular characterization of hasA from an operon required for hyaluronic
RT   acid synthesis in group A streptococci.";
RL   J. Biol. Chem. 269:169-175(1994).
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.
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;
CC   -!- PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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; L21187; AAA17725.1; -; Unassigned_DNA.
DR   RefSeq; WP_011018340.1; NZ_UHHV01000001.1.
DR   AlphaFoldDB; P0C0H0; -.
DR   SMR; P0C0H0; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   TCDB; 4.D.1.1.4; the putative vectorial glycosyl polymerization (vgp) family.
DR   eggNOG; COG1215; Bacteria.
DR   SABIO-RK; P0C0H0; -.
DR   UniPathway; UPA00341; -.
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   GO; GO:0090609; P:single-species submerged biofilm formation; IMP:CACAO.
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_0000197164"
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"
FT   CONFLICT        60
FT                   /note="K -> N (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   419 AA;  47900 MW;  EB173041DA93A71B CRC64;
     MPIFKKTLIV LSFIFLISIL IYLNMYLFGT STVGIYGVIL ITYLVIKLGL SFLYEPFKGK
     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