PGAC_ECOLI
ID PGAC_ECOLI Reviewed; 441 AA.
AC P75905;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
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; Synonyms=ycdQ; OrderedLocusNames=b1022, JW1007;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP ROLE IN THE SYNTHESIS OF A BIOFILM POLYSACCHARIDE, OPERON STRUCTURE, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15090514; DOI=10.1128/jb.186.9.2724-2734.2004;
RA Wang X., Preston J.F. III, Romeo T.;
RT "The pgaABCD locus of Escherichia coli promotes the synthesis of a
RT polysaccharide adhesin required for biofilm formation.";
RL J. Bacteriol. 186:2724-2734(2004).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP FUNCTION IN PGA SYNTHESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18359807; DOI=10.1128/jb.01920-07;
RA Itoh Y., Rice J.D., Goller C., Pannuri A., Taylor J., Meisner J.,
RA Beveridge T.J., Preston J.F. III, Romeo T.;
RT "Roles of pgaABCD genes in synthesis, modification, and export of the
RT Escherichia coli biofilm adhesin poly-beta-1,6-N-acetyl-D-glucosamine.";
RL J. Bacteriol. 190:3670-3680(2008).
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:0000269|PubMed:15090514,
CC ECO:0000269|PubMed:18359807}.
CC -!- INTERACTION:
CC P75905; P69432: pgaD; NbExp=2; IntAct=EBI-561450, EBI-562069;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not synthesize PGA.
CC {ECO:0000269|PubMed:15090514, ECO:0000269|PubMed:18359807}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; U00096; AAC74107.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35803.1; -; Genomic_DNA.
DR PIR; D64844; D64844.
DR RefSeq; NP_415541.1; NC_000913.3.
DR RefSeq; WP_000610451.1; NZ_STEB01000006.1.
DR AlphaFoldDB; P75905; -.
DR SMR; P75905; -.
DR BioGRID; 4260056; 253.
DR ComplexPortal; CPX-3743; pgaCD beta-glycosyltransferase complex.
DR DIP; DIP-11512N; -.
DR IntAct; P75905; 6.
DR MINT; P75905; -.
DR STRING; 511145.b1022; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.1.1.3; the putative vectorial glycosyl polymerization (vgp) family.
DR PaxDb; P75905; -.
DR PRIDE; P75905; -.
DR EnsemblBacteria; AAC74107; AAC74107; b1022.
DR EnsemblBacteria; BAA35803; BAA35803; BAA35803.
DR GeneID; 945606; -.
DR KEGG; ecj:JW1007; -.
DR KEGG; eco:b1022; -.
DR PATRIC; fig|1411691.4.peg.1247; -.
DR EchoBASE; EB3623; -.
DR eggNOG; COG1215; Bacteria.
DR HOGENOM; CLU_023978_0_1_6; -.
DR InParanoid; P75905; -.
DR OMA; WYSLRNC; -.
DR PhylomeDB; P75905; -.
DR BioCyc; EcoCyc:G6529-MON; -.
DR BioCyc; MetaCyc:G6529-MON; -.
DR PRO; PR:P75905; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IMP:EcoCyc.
DR GO; GO:0043708; P:cell adhesion involved in biofilm formation; IDA:ComplexPortal.
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 1: Evidence at protein level;
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_0000059212"
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; 50766 MW; 04F5A53D72FEBABB CRC64;
MINRIVSFFI LCLVLCIPLC VAYFHSGELM MRFVFFWPFF MSIMWIVGGV YFWVYRERHW
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 PLFFEYCLTT IWAFTCLVGF IIYAVQLAGV PLNIELTHIA
ATHTAGILLC TLCLLQFIVS LMIENRYEHN LTSSLFWIIW FPVIFWMLSL ATTLVSFTRV
MLMPKKQRAR WVSPDRGILR G
