ID   ICAA_STAA8              Reviewed;         412 AA.
AC   Q9RQP9; Q2FUU9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 104.
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=SAOUHSC_03002;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ROLE IN BIOFILM FORMATION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=10496925; DOI=10.1128/iai.67.10.5427-5433.1999;
RA   Cramton S.E., Gerke C., Schnell N.F., Nichols W.W., Goetz F.;
RT   "The intercellular adhesion (ica) locus is present in Staphylococcus aureus
RT   and is required for biofilm formation.";
RL   Infect. Immun. 67:5427-5433(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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   -!- DISRUPTION PHENOTYPE: Deletion of the icaADBCR genes leads to the
CC       inability to form biofilms, produce PIA or mediate N-
CC       acetylglucosaminyltransferase activity in vitro.
CC       {ECO:0000269|PubMed:10496925}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; AF086783; AAD52055.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD31989.1; -; Genomic_DNA.
DR   RefSeq; WP_001159430.1; NZ_LS483365.1.
DR   RefSeq; YP_501451.1; NC_007795.1.
DR   AlphaFoldDB; Q9RQP9; -.
DR   SMR; Q9RQP9; -.
DR   STRING; 1280.SAXN108_2939; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ABD31989; ABD31989; SAOUHSC_03002.
DR   GeneID; 3921484; -.
DR   KEGG; sao:SAOUHSC_03002; -.
DR   PATRIC; fig|93061.5.peg.2709; -.
DR   eggNOG; COG1215; Bacteria.
DR   HOGENOM; CLU_023978_0_1_9; -.
DR   OMA; RNRWAEG; -.
DR   PRO; PR:Q9RQP9; -.
DR   Proteomes; UP000008816; 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; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..412
FT                   /note="Poly-beta-1,6-N-acetyl-D-glucosamine synthase"
FT                   /id="PRO_0000059275"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        396
FT                   /note="K -> R (in Ref. 1; AAD52055)"
FT                   /evidence="ECO:0000305"
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