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Protein

Poly-beta-1,6-N-acetyl-D-glucosamine export protein

Gene

pgaA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • substrate-specific transmembrane transporter activity Source: EcoCyc

GO - Biological processi

  • single-species biofilm formation Source: EcoCyc
  • transport Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

BioCyciEcoCyc:G6531-MONOMER.
ECOL316407:JW1010-MONOMER.
MetaCyc:G6531-MONOMER.
BRENDAi3.1.1.58. 2026.

Protein family/group databases

TCDBi1.B.55.1.1. the poly acetyl glucosamine porin (pgaa) family.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:pgaA
Synonyms:ycdS
Ordered Locus Names:b1024, JW1010
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13865. pgaA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 807781Poly-beta-1,6-N-acetyl-D-glucosamine export proteinPRO_0000035694Add
BLAST

Proteomic databases

PaxDbiP69434.
PRIDEiP69434.

Expressioni

Inductioni

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.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi4263226. 121 interactions.
IntActiP69434. 1 interaction.
STRINGi511145.b1024.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi518 – 53013Combined sources
Beta strandi540 – 5478Combined sources
Beta strandi551 – 56515Combined sources
Beta strandi574 – 58613Combined sources
Beta strandi589 – 59911Combined sources
Beta strandi604 – 61714Combined sources
Beta strandi620 – 62910Combined sources
Helixi638 – 6403Combined sources
Beta strandi644 – 67027Combined sources
Beta strandi675 – 68915Combined sources
Beta strandi691 – 6977Combined sources
Beta strandi700 – 7056Combined sources
Beta strandi717 – 7237Combined sources
Beta strandi725 – 73511Combined sources
Beta strandi738 – 75316Combined sources
Turni754 – 7563Combined sources
Beta strandi757 – 77216Combined sources
Turni773 – 7753Combined sources
Beta strandi776 – 80732Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Y25X-ray2.82A511-807[»]
ProteinModelPortaliP69434.
SMRiP69434. Positions 42-165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati98 – 13134TPR 1Add
BLAST
Repeati165 – 19834TPR 2Add
BLAST
Repeati279 – 31133TPR 3Add
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, TPR repeat, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4108TUY. Bacteria.
ENOG4111HEP. LUCA.
HOGENOMiHOG000118896.
KOiK11935.
OMAiIDAVLYS.
OrthoDBiEOG64N9S4.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR023870. PGA_export_porin_PgaA.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
SMARTiSM00028. TPR. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
TIGRFAMsiTIGR03939. PGA_TPR_OMP. 1 hit.
PROSITEiPS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P69434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYSSSRKRCP KTKWALKLLT AAFLAASPAA KSAVNNAYDA LIIEARKGNT
60 70 80 90 100
QPALSWFALK SALSNNQIAD WLQIALWAGQ DKQVITVYNR YRHQQLPARG
110 120 130 140 150
YAAVAVAYRN LQQWQNSLTL WQKALSLEPQ NKDYQRGQIL TLADAGHYDT
160 170 180 190 200
ALVKLKQLNS GAPDKANLLA EAYIYKLAGR HQDELRAMTE SLPENASTQQ
210 220 230 240 250
YPTEYVQALR NNQLAAAIDD ANLTPDIRAD IHAELVRLSF MPTRSESERY
260 270 280 290 300
AIADRALAQY AALEILWHDN PDRTAQYQRI QVDHLGALLT RDRYKDVISH
310 320 330 340 350
YQRLKKTGQI IPPWGQYWVA SAYLKDHQPK KAQSIMTELF YHKETIAPDL
360 370 380 390 400
SDEELADLFY SHLESENYPG ALTVTQHTIN TSPPFLRLMG TPTSIPNDTW
410 420 430 440 450
LQGHSFLSTV AKYSNDLPQA EMTARELAYN APGNQGLRID YASVLQARGW
460 470 480 490 500
PRAAENELKK AEVIEPRNIN LEVEQAWTAL TLQEWQQAAV LTHDVVEREP
510 520 530 540 550
QDPGVVRLKR AVDVHNLAEL RIAGSTGIDA EGPDSGKHDV DLTTIVYSPP
560 570 580 590 600
LKDNWRGFAG FGYADGQFSE GKGIVRDWLA GVEWRSRNIW LEAEYAERVF
610 620 630 640 650
NHEHKPGARL SGWYDFNDNW RIGSQLERLS HRVPLRAMKN GVTGNSAQAY
660 670 680 690 700
VRWYQNERRK YGVSWAFTDF SDSNQRHEVS LEGQERIWSS PYLIVDFLPS
710 720 730 740 750
LYYEQNTEHD TPYYNPIKTF DIVPAFEASH LLWRSYENSW EQIFSAGVGA
760 770 780 790 800
SWQKHYGTDV VTQLGYGQRI SWNDVIDAGA TLRWEKRPYD GDREHNLYVE

FDMTFRF
Length:807
Mass (Da):92,207
Last modified:March 1, 2005 - v1
Checksum:iB20067C3D41723FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74109.1.
AP009048 Genomic DNA. Translation: BAA35806.1.
PIRiF64844.
RefSeqiNP_415543.1. NC_000913.3.
WP_000287458.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74109; AAC74109; b1024.
BAA35806; BAA35806; BAA35806.
GeneIDi945596.
KEGGiecj:JW1010.
eco:b1024.
PATRICi32117281. VBIEscCol129921_1064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74109.1.
AP009048 Genomic DNA. Translation: BAA35806.1.
PIRiF64844.
RefSeqiNP_415543.1. NC_000913.3.
WP_000287458.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Y25X-ray2.82A511-807[»]
ProteinModelPortaliP69434.
SMRiP69434. Positions 42-165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263226. 121 interactions.
IntActiP69434. 1 interaction.
STRINGi511145.b1024.

Protein family/group databases

TCDBi1.B.55.1.1. the poly acetyl glucosamine porin (pgaa) family.

Proteomic databases

PaxDbiP69434.
PRIDEiP69434.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74109; AAC74109; b1024.
BAA35806; BAA35806; BAA35806.
GeneIDi945596.
KEGGiecj:JW1010.
eco:b1024.
PATRICi32117281. VBIEscCol129921_1064.

Organism-specific databases

EchoBASEiEB3625.
EcoGeneiEG13865. pgaA.

Phylogenomic databases

eggNOGiENOG4108TUY. Bacteria.
ENOG4111HEP. LUCA.
HOGENOMiHOG000118896.
KOiK11935.
OMAiIDAVLYS.
OrthoDBiEOG64N9S4.

Enzyme and pathway databases

BioCyciEcoCyc:G6531-MONOMER.
ECOL316407:JW1010-MONOMER.
MetaCyc:G6531-MONOMER.
BRENDAi3.1.1.58. 2026.

Miscellaneous databases

PROiP69434.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR023870. PGA_export_porin_PgaA.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
SMARTiSM00028. TPR. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 2 hits.
TIGRFAMsiTIGR03939. PGA_TPR_OMP. 1 hit.
PROSITEiPS50005. TPR. 1 hit.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. 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.

Entry informationi

Entry nameiPGAA_ECOLI
AccessioniPrimary (citable) accession number: P69434
Secondary accession number(s): P75907
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: July 6, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.