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P69434 (PGAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=PGA export protein
Short name=Poly-beta-1,6-GlcNAc export protein
Gene names
Name:pgaA
Synonyms:ycdS
Ordered Locus Names:b1024, JW1010
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length807 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exports the biofilm adhesin polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PGA) across the outer membrane. The PGA transported seems to be partially N-deacetylated since N-deacetylation of PGA by PgaB is needed for PGA export through the PgaA porin. Ref.4 Ref.5 Ref.6

Required for the synthesis of the beta-1,6-GlcNAc polysaccharide (PGA or poly-GlcNAc) that seems to serve as a biofilm adhesin. Ref.4 Ref.5 Ref.6

Subcellular location

Cell outer membrane; Multi-pass membrane protein Probable Ref.5.

Induction

Levels of this protein are negatively controlled by the second messenger ppGpp (at protein level) at a post-transcriptional level. Increased levels of c-di-GMP lead to decreased levels of PgaA. Ref.6

Domain

Contains a predicted C-terminal beta-barrel porin domain and a N-terminal periplasmic superhelical domain containing tetratricopeptide repeats, which may mediate protein-protein interactions, perhaps with PgaB. Ref.5

Disruption phenotype

Deletion of pgaA does not prevent PGA synthesis but does block its export. The synthesized PGA is retained in the periplasm and accumulates at the cell poles. Disruption of the pga operon causes severe and persistent defects in the biofilm formation process. Ref.4 Ref.5

Sequence similarities

Contains 3 TPR repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 807781Poly-beta-1,6-N-acetyl-D-glucosamine export protein
PRO_0000035694

Regions

Repeat98 – 13134TPR 1
Repeat165 – 19834TPR 2
Repeat279 – 31133TPR 3

Sequences

Sequence LengthMass (Da)Tools
P69434 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: B20067C3D41723FD

FASTA80792,207
        10         20         30         40         50         60 
MYSSSRKRCP KTKWALKLLT AAFLAASPAA KSAVNNAYDA LIIEARKGNT QPALSWFALK 

        70         80         90        100        110        120 
SALSNNQIAD WLQIALWAGQ DKQVITVYNR YRHQQLPARG YAAVAVAYRN LQQWQNSLTL 

       130        140        150        160        170        180 
WQKALSLEPQ NKDYQRGQIL TLADAGHYDT ALVKLKQLNS GAPDKANLLA EAYIYKLAGR 

       190        200        210        220        230        240 
HQDELRAMTE SLPENASTQQ YPTEYVQALR NNQLAAAIDD ANLTPDIRAD IHAELVRLSF 

       250        260        270        280        290        300 
MPTRSESERY AIADRALAQY AALEILWHDN PDRTAQYQRI QVDHLGALLT RDRYKDVISH 

       310        320        330        340        350        360 
YQRLKKTGQI IPPWGQYWVA SAYLKDHQPK KAQSIMTELF YHKETIAPDL SDEELADLFY 

       370        380        390        400        410        420 
SHLESENYPG ALTVTQHTIN TSPPFLRLMG TPTSIPNDTW LQGHSFLSTV AKYSNDLPQA 

       430        440        450        460        470        480 
EMTARELAYN APGNQGLRID YASVLQARGW PRAAENELKK AEVIEPRNIN LEVEQAWTAL 

       490        500        510        520        530        540 
TLQEWQQAAV LTHDVVEREP QDPGVVRLKR AVDVHNLAEL RIAGSTGIDA EGPDSGKHDV 

       550        560        570        580        590        600 
DLTTIVYSPP LKDNWRGFAG FGYADGQFSE GKGIVRDWLA GVEWRSRNIW LEAEYAERVF 

       610        620        630        640        650        660 
NHEHKPGARL SGWYDFNDNW RIGSQLERLS HRVPLRAMKN GVTGNSAQAY VRWYQNERRK 

       670        680        690        700        710        720 
YGVSWAFTDF SDSNQRHEVS LEGQERIWSS PYLIVDFLPS LYYEQNTEHD TPYYNPIKTF 

       730        740        750        760        770        780 
DIVPAFEASH LLWRSYENSW EQIFSAGVGA SWQKHYGTDV VTQLGYGQRI SWNDVIDAGA 

       790        800 
TLRWEKRPYD GDREHNLYVE FDMTFRF 

« 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]"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 EXPORT, DOMAIN, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
Strain: K12 / MG1655 / ATCC 47076.
[6]"Second messenger signalling governs Escherichia coli biofilm induction upon ribosomal stress."
Boehm A., Steiner S., Zaehringer F., Casanova A., Hamburger F., Ritz D., Keck W., Ackermann M., Schirmer T., Jenal U.
Mol. Microbiol. 72:1500-1516(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN BIOFILM FORMATION, INDUCTION.
Strain: K12 / MG1655 / AB400.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC74109.1.
AP009048 Genomic DNA. Translation: BAA35806.1.
PIRF64844.
RefSeqNP_415543.1. NC_000913.2.
YP_489295.1. NC_007779.1.

3D structure databases

ProteinModelPortalP69434.
ModBaseSearch...

Protein-protein interaction databases

IntActP69434. 1 interaction.
STRING511145.b1024.

Protein family/group databases

TCDB1.B.55.1.1. poly acetyl glucosamine porin (PgaA) family.

Proteomic databases

PaxDbP69434.
PRIDEP69434.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74109; AAC74109; b1024.
BAA35806; BAA35806; BAA35806.
GeneID12934232.
945596.
KEGGecj:Y75_p0996.
eco:b1024.
PATRIC32117281. VBIEscCol129921_1064.

Organism-specific databases

EchoBASEEB3625.
EcoGeneEG13865. pgaA.

Phylogenomic databases

eggNOGNOG06511.
HOGENOMHOG000118896.
KOK11935.
OMALWRHYER.
ProtClustDBPRK10049.

Enzyme and pathway databases

BioCycEcoCyc:G6531-MONOMER.
ECOL316407:JW1010-MONOMER.

Gene expression databases

GenevestigatorP69434.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
InterProIPR023870. PGA_export_porin_PgaA.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
TIGRFAMsTIGR03939. PGA_TPR_OMP. 1 hit.
PROSITEPS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGAA_ECOLI
AccessionPrimary (citable) accession number: P69434
Secondary accession number(s): P75907
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: May 1, 2013
This is version 70 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