HASA_STRP8
ID HASA_STRP8 Reviewed; 419 AA.
AC Q8NKX1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=spyM18_2236;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18 group
RT A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(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.
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; AE009949; AAL98667.1; -; Genomic_DNA.
DR PIR; A53100; A53100.
DR RefSeq; WP_011018340.1; NC_003485.1.
DR AlphaFoldDB; Q8NKX1; -.
DR SMR; Q8NKX1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR KEGG; spm:spyM18_2236; -.
DR HOGENOM; CLU_029695_4_0_9; -.
DR OMA; DVIVPCF; -.
DR UniPathway; UPA00341; -.
DR PHI-base; PHI:5099; -.
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_0000197168"
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; 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