PGAC_ECO57
ID PGAC_ECO57 Reviewed; 441 AA.
AC Q8XAR5; Q7AFM3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Poly-beta-1,6-N-acetyl-D-glucosamine synthase;
DE Short=PGA synthase;
DE Short=Poly-beta-1,6-GlcNAc synthase;
DE EC=2.4.1.-;
DE AltName: Full=Biofilm PGA synthesis protein PgaC;
DE AltName: Full=N-acetylglucosaminyltransferase PgaC;
GN Name=pgaC; OrderedLocusNames=Z1524, ECs1268;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Probable 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 (PGA),
CC a biofilm adhesin polysaccharide. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AE005174; AAG55640.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34691.1; -; Genomic_DNA.
DR PIR; D85647; D85647.
DR PIR; D90787; D90787.
DR RefSeq; NP_309295.1; NC_002695.1.
DR RefSeq; WP_000610461.1; NZ_SEKU01000016.1.
DR AlphaFoldDB; Q8XAR5; -.
DR SMR; Q8XAR5; -.
DR STRING; 155864.EDL933_1449; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; AAG55640; AAG55640; Z1524.
DR EnsemblBacteria; BAB34691; BAB34691; ECs_1268.
DR GeneID; 912769; -.
DR KEGG; ece:Z1524; -.
DR KEGG; ecs:ECs_1268; -.
DR PATRIC; fig|386585.9.peg.1376; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_023978_0_1_6; -.
DR OMA; WYSLRNC; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 inner membrane; Cell membrane; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..441
FT /note="Poly-beta-1,6-N-acetyl-D-glucosamine synthase"
FT /id="PRO_0000059213"
FT TOPO_DOM 1..4
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..330
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..394
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 441 AA; 50769 MW; 17E7AC76C5BB6FA8 CRC64;
MINRIVSFFI LCLVLCIPLC VAYFHSGELM MRFVFFWPFF MSIMWIVGGV YFWVYRERRW
PWGENAPAPQ LKDNPSISII IPCFNEEKNV EETIHAALAQ RYENIEVIAV NDGSTDKTRA
ILDRMAAQIP HLRVIHLAQN QGKAIALKTG AAAAKSEYLV CIDGDALLDR DAAAYIVEPM
LYNPRVGAVT GNPRIRTRST LVGKIQVGEY SSIIGLIKRT QRIYGNVFTV SGVIAAFRRS
ALAEVGYWSD DMITEDIDIS WKLQLNQWTI FYEPRALCWI LMPETLKGLW KQRLRWAQGG
AEVFLKNMTR LWRKENFRMW PLFFEYSLTT IWAFTCLVGF IIYAVQLAGV PLNIELTHIA
ATHTAGILLC TLCLLQFIVS LMIENRYEHN LTSSLFWIIW FPVIFWMLSL ATTLVSFTRV
MLMPKKQRAR WVSPDRGILR G
