ID   ICAA_STAAR              Reviewed;         412 AA.
AC   Q6GDD8;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Poly-beta-1,6-N-acetyl-D-glucosamine synthase;
DE            Short=PNAG synthase;
DE            Short=Poly-beta-1,6-GlcNAc synthase;
DE            EC=2.4.1.-;
DE   AltName: Full=Biofilm polysaccharide intercellular adhesin synthesis protein IcaA;
DE            Short=Biofilm PIA synthesis protein IcaA;
DE   AltName: Full=Intercellular adhesion protein A;
DE   AltName: Full=N-acetylglucosaminyltransferase IcaA;
GN   Name=icaA; OrderedLocusNames=SAR2747;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: N-acetylglucosaminyltransferase that catalyzes the
CC       polymerization of single monomer units of UDP-N-acetylglucosamine to
CC       produce the linear homomer poly-beta-1,6-N-acetyl-D-glucosamine (PNAG,
CC       also referred to as PIA), a biofilm adhesin polysaccharide. Requires
CC       IcaD for full activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; BX571856; CAG41723.1; -; Genomic_DNA.
DR   RefSeq; WP_001159430.1; NC_002952.2.
DR   AlphaFoldDB; Q6GDD8; -.
DR   SMR; Q6GDD8; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   KEGG; sar:SAR2747; -.
DR   HOGENOM; CLU_023978_0_1_9; -.
DR   OMA; RNRWAEG; -.
DR   OrthoDB; 724641at2; -.
DR   Proteomes; UP000000596; 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:0008375; F:acetylglucosaminyltransferase activity; IEA:InterPro.
DR   GO; GO:0043708; P:cell adhesion involved in biofilm formation; IEA:InterPro.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR023853; PGA_PgaC/IcaA.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03937; PgaC_IcaA; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..412
FT                   /note="Poly-beta-1,6-N-acetyl-D-glucosamine synthase"
FT                   /id="PRO_0000059279"
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   412 AA;  47770 MW;  9A68805152695BB4 CRC64;
     MQFFNFLLFY PVFMSIYWIV GSIYFYFTRE IRYSLNKKPD INVDELEGIT FLLACYNESE
     TIEDTLSNVL ALKYEKKEII IINDGSSDNT AELIYKIKEN NDFIFVDLQE NRGKANALNQ
     GIKQASYDYV MCLDADTIVD QDAPYYMIEN FKHDPKLGAV TGNPRIRNKS SILGKIQTIE
     YASLIGCIKR SQTLAGAVNT ISGVFTLFKK SAVVDVGYWD TDMITEDIAV SWKLHLRGYR
     IKYEPLAMCW MLVPETLGGL WKQRVRWAQG GHEVLLRDFF STMKTKRFPL YILMFEQIIS
     ILWVYIVLLY LGYLFITANF LDYTFMTYSF SIFLLSSFTM TFINVIQFTV ALFIDSRYEK
     KNMAGLIFVS WYPTVYWIIN AAVVLVAFPK ALKRKKGGYA TWSSPDRGNT QR