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P75906 (PGAB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 N-deacetylase
Short name=PGA N-deacetylase
Short name=Poly-beta-1,6-GlcNAc N-deacetylase
EC=3.5.1.-
Gene names
Name:pgaB
Synonyms:ycdR
Ordered Locus Names:b1023, JW5142
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length672 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PGA), a biofilm adhesin polysaccharide. N-deacetylation promotes PGA export through the PgaA porin. Ref.4 Ref.5

Subcellular location

Cell outer membrane; Lipid-anchor; Periplasmic side Probable Ref.5.

Domain

Contains a N-terminal polysaccharide deacetylase domain, and a C-terminal domain required for PGA N-deacetylation that may be involved in binding to unmodified poly-beta-1,6-GlcNAc and thereby assists catalysis by the deacetylase domain. Ref.5

Disruption phenotype

Deletion of pgaB does not prevent PGA synthesis but does block its export and biofilm formation. The synthesized PGA is retained in the periplasm and accumulates at the cell poles. Ref.4 Ref.5

Sequence similarities

Belongs to the polysaccharide deacetylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 672652Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase
PRO_0000024844

Amino acid modifications

Lipidation211N-palmitoyl cysteine Potential
Lipidation211S-diacylglycerol cysteine Potential

Experimental info

Mutagenesis1151D → A: High decrease in catalytic activity. Unable to support biofilm formation and PGA secretion. Ref.5
Mutagenesis1841H → A: Unable to support biofilm formation and PGA secretion. Ref.5

Secondary structure

1 .......................................................................................................... 672
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P75906 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 8B68D0FFB657F4F2

FASTA67277,413
        10         20         30         40         50         60 
MLRNGNKYLL MLVSIIMLTA CISQSRTSFI PPQDRESLLA EQPWPHNGFV AISWHNVEDE 

        70         80         90        100        110        120 
AADQRFMSVR TSALREQFAW LRENGYQPVS IAQIREAHRG GKPLPEKAVV LTFDDGYQSF 

       130        140        150        160        170        180 
YTRVFPILQA FQWPAVWAPV GSWVDTPADK QVKFGDELVD REYFATWQQV REVARSRLVE 

       190        200        210        220        230        240 
LASHTWNSHY GIQANATGSL LPVYVNRAYF TDHARYETAA EYRERIRLDA VKMTEYLRTK 

       250        260        270        280        290        300 
VEVNPHVFVW PYGEANGIAI EELKKLGYDM FFTLESGLAN ASQLDSIPRV LIANNPSLKE 

       310        320        330        340        350        360 
FAQQIITVQE KSPQRIMHID LDYVYDENLQ QMDRNIDVLI QRVKDMQIST VYLQAFADPD 

       370        380        390        400        410        420 
GDGLVKEVWF PNRLLPMKAD IFSRVAWQLR TRSGVNIYAW MPVLSWDLDP TLTRVKYLPT 

       430        440        450        460        470        480 
GEKKAQIHPE QYHRLSPFDD RVRAQVGMLY EDLAGHAAFD GILFHDDALL SDYEDASAPA 

       490        500        510        520        530        540 
ITAYQQAGFS GSLSEIRQNP EQFKQWARFK SRALTDFTLE LSARVKAIRG PHIKTARNIF 

       550        560        570        580        590        600 
ALPVIQPESE AWFAQNYADF LKSYDWTAIM AMPYLEGVAE KSADQWLIQL TNQIKNIPQA 

       610        620        630        640        650        660 
KDKSILELQA QNWQKNGQHQ AISSQQLAHW MSLLQLNGVK NYGYYPDNFL HNQPEIDLIR 

       670 
PEFSTAWYPK ND

« 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], SEQUENCE REVISION.
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 AS A PGA DEACETYLASE, MUTAGENESIS OF ASP-115 AND HIS-184, DOMAIN, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
Strain: K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U00096 Genomic DNA. Translation: AAC74108.1.
AP009048 Genomic DNA. Translation: BAA35805.2.
PIRE64844.
RefSeqNP_415542.1. NC_000913.2.
YP_489294.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VUSX-ray1.65A/B42-309[»]
4F9DX-ray1.90A/B42-655[»]
4F9JX-ray2.10A/B42-655[»]
ProteinModelPortalP75906.
SMRP75906. Positions 43-649.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-11513N.
STRING511145.b1023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74108; AAC74108; b1023.
BAA35805; BAA35805; BAA35805.
GeneID12931056.
945604.
KEGGecj:Y75_p0995.
eco:b1023.
PATRIC32117279. VBIEscCol129921_1063.

Organism-specific databases

EchoBASEEB3624.
EcoGeneEG13864. pgaB.

Phylogenomic databases

eggNOGCOG0726.
HOGENOMHOG000170240.
KOK11931.
OMAHVDLDYV.
ProtClustDBPRK14582.

Enzyme and pathway databases

BioCycEcoCyc:G6530-MONOMER.
ECOL316407:JW5142-MONOMER.
MetaCyc:G6530-MONOMER.

Gene expression databases

GenevestigatorP75906.

Family and domain databases

Gene3D3.20.20.370. 1 hit.
InterProIPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR023854. PGA_deacetylase_PgaB.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamPF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SUPFAMSSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.
TIGRFAMsTIGR03938. deacetyl_PgaB. 1 hit.
PROSITEPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGAB_ECOLI
AccessionPrimary (citable) accession number: P75906
Secondary accession number(s): Q9R7P5, Q9R7P7, Q9R7P8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 1, 2013
This is version 105 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents