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P75905 (PGAC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Poly-beta-1,6-N-acetyl-D-glucosamine synthase

Short name=PGA synthase
Short name=Poly-beta-1,6-GlcNAc synthase
EC=2.4.1.-
Alternative name(s):
Biofilm PGA synthesis protein PgaC
N-acetylglucosaminyltransferase PgaC
Gene names
Name:pgaC
Synonyms:ycdQ
Ordered Locus Names:b1022, JW1007
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable N-acetylglucosaminyltransferase that catalyzes the polymerization of single monomer units of UDP-N-acetylglucosamine to produce the linear homopolymer poly-beta-1,6-N-acetyl-D-glucosamine (PGA), a biofilm adhesin polysaccharide. Ref.4 Ref.6

Subcellular location

Cell inner membrane; Multi-pass membrane protein.

Disruption phenotype

Cells lacking this gene do not synthesize PGA. Ref.4 Ref.6

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441Poly-beta-1,6-N-acetyl-D-glucosamine synthase
PRO_0000059212

Regions

Topological domain1 – 44Periplasmic Potential
Transmembrane5 – 2521Helical; Potential
Topological domain26 – 327Cytoplasmic Potential
Transmembrane33 – 5321Helical; Potential
Topological domain54 – 330277Periplasmic Potential
Transmembrane331 – 35121Helical; Potential
Topological domain352 – 36211Cytoplasmic Potential
Transmembrane363 – 38321Helical; Potential
Topological domain384 – 39411Periplasmic Potential
Transmembrane395 – 41521Helical; Potential
Topological domain416 – 44126Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
P75905 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 04F5A53D72FEBABB

FASTA44150,766
        10         20         30         40         50         60 
MINRIVSFFI LCLVLCIPLC VAYFHSGELM MRFVFFWPFF MSIMWIVGGV YFWVYRERHW 

        70         80         90        100        110        120 
PWGENAPAPQ LKDNPSISII IPCFNEEKNV EETIHAALAQ RYENIEVIAV NDGSTDKTRA 

       130        140        150        160        170        180 
ILDRMAAQIP HLRVIHLAQN QGKAIALKTG AAAAKSEYLV CIDGDALLDR DAAAYIVEPM 

       190        200        210        220        230        240 
LYNPRVGAVT GNPRIRTRST LVGKIQVGEY SSIIGLIKRT QRIYGNVFTV SGVIAAFRRS 

       250        260        270        280        290        300 
ALAEVGYWSD DMITEDIDIS WKLQLNQWTI FYEPRALCWI LMPETLKGLW KQRLRWAQGG 

       310        320        330        340        350        360 
AEVFLKNMTR LWRKENFRMW PLFFEYCLTT IWAFTCLVGF IIYAVQLAGV PLNIELTHIA 

       370        380        390        400        410        420 
ATHTAGILLC TLCLLQFIVS LMIENRYEHN LTSSLFWIIW FPVIFWMLSL ATTLVSFTRV 

       430        440 
MLMPKKQRAR WVSPDRGILR G 

« Hide

References

« Hide 'large scale' references
[1]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The pgaABCD locus of Escherichia coli promotes the synthesis of a polysaccharide adhesin required for biofilm formation."
Wang X., Preston J.F. III, Romeo T.
J. Bacteriol. 186:2724-2734(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN THE SYNTHESIS OF A BIOFILM POLYSACCHARIDE, OPERON STRUCTURE, DISRUPTION PHENOTYPE.
Strain: K12 / MG1655 / ATCC 47076.
[5]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.
[6]"Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-beta-1,6-N-acetyl-D-glucosamine."
Itoh Y., Rice J.D., Goller C., Pannuri A., Taylor J., Meisner J., Beveridge T.J., Preston J.F. III, Romeo T.
J. Bacteriol. 190:3670-3680(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PGA SYNTHESIS, DISRUPTION PHENOTYPE.
Strain: K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC74107.1.
AP009048 Genomic DNA. Translation: BAA35803.1.
PIRD64844.
RefSeqNP_415541.1. NC_000913.2.
YP_489293.1. NC_007779.1.

3D structure databases

ProteinModelPortalP75905.
SMRP75905. Positions 67-334.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-11512N.
IntActP75905. 5 interactions.
MINTMINT-1234361.
STRING511145.b1022.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.
TCDB9.B.32.1.3. putative vectorial glycosyl polymerization (VGP) family.

Proteomic databases

PaxDbP75905.
PRIDEP75905.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74107; AAC74107; b1022.
BAA35803; BAA35803; BAA35803.
GeneID12931062.
945606.
KEGGecj:Y75_p0994.
eco:b1022.
PATRIC32117277. VBIEscCol129921_1062.

Organism-specific databases

EchoBASEEB3623.
EcoGeneEG13863. pgaC.

Phylogenomic databases

eggNOGCOG1215.
HOGENOMHOG000170129.
KOK11936.
OMALVSFPKV.
ProtClustDBPRK11204.

Enzyme and pathway databases

BioCycEcoCyc:G6529-MONOMER.
ECOL316407:JW1007-MONOMER.
MetaCyc:G6529-MONOMER.

Gene expression databases

GenevestigatorP75905.

Family and domain databases

InterProIPR001173. Glyco_trans_2.
IPR023853. PGA_PgaC/IcaA.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR03937. PgaC_IcaA. 1 hit.
ProtoNetSearch...

Entry information

Entry namePGAC_ECOLI
AccessionPrimary (citable) accession number: P75905
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families