HASA_STRP1
ID HASA_STRP1 Reviewed; 419 AA.
AC P0C0H1; Q08494; Q48W06; Q54865; Q54868;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=SPy_2200, M5005_Spy1851;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK34828.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ52469.1; -; Genomic_DNA.
DR RefSeq; NP_270107.2; NC_002737.2.
DR AlphaFoldDB; P0C0H1; -.
DR SMR; P0C0H1; -.
DR STRING; 1314.HKU360_01961; -.
DR PaxDb; P0C0H1; -.
DR EnsemblBacteria; AAK34828; AAK34828; SPy_2200.
DR KEGG; spy:SPy_2200; -.
DR KEGG; spz:M5005_Spy1851; -.
DR PATRIC; fig|160490.10.peg.1905; -.
DR HOGENOM; CLU_029695_4_0_9; -.
DR OMA; DVIVPCF; -.
DR UniPathway; UPA00341; -.
DR Proteomes; UP000000750; 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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..419
FT /note="Hyaluronan synthase"
FT /id="PRO_0000197165"
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 10
FT /note="V -> I (in Ref. 2; AAZ52469)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="K -> R (in Ref. 2; AAZ52469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 47886 MW; A6AFE04B54B8D385 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
SFFKESIISV KKILSNPIVA LWTIFEVVMF MMLIVAIGNL LFNQAIQLDL IKLFAFLSII
FIVALCRNVH YMIKHPASFL LSPLYGILHL FVLQPLKLYS LCTIKNTEWG TRKKVTIFK
