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P75906

- PGAB_ECOLI

UniProt

P75906 - PGAB_ECOLI

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Protein
Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase
Gene
pgaB, ycdR, b1023, JW5142
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. biofilm formation Source: EcoCyc
  2. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase (EC:3.5.1.-)
Short name:
PGA N-deacetylase
Short name:
Poly-beta-1,6-GlcNAc N-deacetylase
Gene namesi
Name:pgaB
Synonyms:ycdR
Ordered Locus Names:b1023, JW5142
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG13864. pgaB.

Subcellular locationi

Cell outer membrane; Lipid-anchor; Periplasmic side Inferred 1 Publication

GO - Cellular componenti

  1. cell outer membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi115 – 1151D → A: High decrease in catalytic activity. Unable to support biofilm formation and PGA secretion. 1 Publication
Mutagenesisi184 – 1841H → A: Unable to support biofilm formation and PGA secretion. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed prediction
Add
BLAST
Chaini21 – 672652Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase
PRO_0000024844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi21 – 211N-palmitoyl cysteine Reviewed prediction
Lipidationi21 – 211S-diacylglycerol cysteine Reviewed prediction

Keywords - PTMi

Lipoprotein, Palmitate

Expressioni

Gene expression databases

GenevestigatoriP75906.

Interactioni

Protein-protein interaction databases

DIPiDIP-11513N.
STRINGi511145.b1023.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 547
Beta strandi57 – 604
Helixi64 – 663
Beta strandi68 – 703
Helixi71 – 8313
Helixi91 – 988
Beta strandi108 – 1158
Helixi118 – 13114
Beta strandi135 – 1395
Helixi141 – 1444
Beta strandi148 – 1503
Beta strandi152 – 1543
Beta strandi157 – 1593
Helixi161 – 1633
Helixi167 – 1759
Beta strandi178 – 1814
Beta strandi190 – 1934
Beta strandi200 – 2023
Helixi203 – 2053
Turni211 – 2144
Helixi219 – 24022
Beta strandi247 – 2493
Helixi251 – 2533
Helixi257 – 2659
Beta strandi270 – 2723
Beta strandi285 – 2873
Helixi298 – 3069
Turni307 – 3093
Beta strandi315 – 3195
Helixi321 – 3244
Helixi329 – 34517
Beta strandi350 – 3545
Beta strandi367 – 3704
Beta strandi373 – 3753
Helixi382 – 39312
Beta strandi396 – 4016
Helixi419 – 4213
Helixi422 – 4265
Helixi429 – 4335
Helixi440 – 45617
Beta strandi460 – 4645
Helixi478 – 4869
Helixi493 – 4975
Helixi500 – 52930
Beta strandi534 – 5407
Helixi541 – 5455
Helixi547 – 5526
Helixi557 – 5637
Beta strandi565 – 5706
Helixi572 – 5754
Helixi580 – 59516
Helixi600 – 6034
Beta strandi604 – 6085
Helixi622 – 63514
Turni636 – 6383
Beta strandi641 – 6444

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VUSX-ray1.65A/B42-309[»]
4F9DX-ray1.90A/B42-655[»]
4F9JX-ray2.10A/B42-655[»]
ProteinModelPortaliP75906.
SMRiP75906. Positions 43-649.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini107 – 349243NodB homology
Add
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0726.
HOGENOMiHOG000170240.
KOiK11931.
OMAiELQTVDW.
OrthoDBiEOG6D8B8W.

Family and domain databases

Gene3Di3.20.20.370. 1 hit.
InterProiIPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR023854. PGA_deacetylase_PgaB.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamiPF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SUPFAMiSSF88713. SSF88713. 2 hits.
TIGRFAMsiTIGR03938. deacetyl_PgaB. 1 hit.
PROSITEiPS51677. NODB. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P75906-1 [UniParc]FASTAAdd to Basket

« Hide

MLRNGNKYLL MLVSIIMLTA CISQSRTSFI PPQDRESLLA EQPWPHNGFV    50
AISWHNVEDE AADQRFMSVR TSALREQFAW LRENGYQPVS IAQIREAHRG 100
GKPLPEKAVV LTFDDGYQSF YTRVFPILQA FQWPAVWAPV GSWVDTPADK 150
QVKFGDELVD REYFATWQQV REVARSRLVE LASHTWNSHY GIQANATGSL 200
LPVYVNRAYF TDHARYETAA EYRERIRLDA VKMTEYLRTK VEVNPHVFVW 250
PYGEANGIAI EELKKLGYDM FFTLESGLAN ASQLDSIPRV LIANNPSLKE 300
FAQQIITVQE KSPQRIMHID LDYVYDENLQ QMDRNIDVLI QRVKDMQIST 350
VYLQAFADPD GDGLVKEVWF PNRLLPMKAD IFSRVAWQLR TRSGVNIYAW 400
MPVLSWDLDP TLTRVKYLPT GEKKAQIHPE QYHRLSPFDD RVRAQVGMLY 450
EDLAGHAAFD GILFHDDALL SDYEDASAPA ITAYQQAGFS GSLSEIRQNP 500
EQFKQWARFK SRALTDFTLE LSARVKAIRG PHIKTARNIF ALPVIQPESE 550
AWFAQNYADF LKSYDWTAIM AMPYLEGVAE KSADQWLIQL TNQIKNIPQA 600
KDKSILELQA QNWQKNGQHQ AISSQQLAHW MSLLQLNGVK NYGYYPDNFL 650
HNQPEIDLIR PEFSTAWYPK ND 672
Length:672
Mass (Da):77,413
Last modified:February 1, 1997 - v1
Checksum:i8B68D0FFB657F4F2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC74108.1.
AP009048 Genomic DNA. Translation: BAA35805.2.
PIRiE64844.
RefSeqiNP_415542.1. NC_000913.3.
YP_489294.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74108; AAC74108; b1023.
BAA35805; BAA35805; BAA35805.
GeneIDi12931056.
945604.
KEGGiecj:Y75_p0995.
eco:b1023.
PATRICi32117279. VBIEscCol129921_1063.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC74108.1 .
AP009048 Genomic DNA. Translation: BAA35805.2 .
PIRi E64844.
RefSeqi NP_415542.1. NC_000913.3.
YP_489294.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3VUS X-ray 1.65 A/B 42-309 [» ]
4F9D X-ray 1.90 A/B 42-655 [» ]
4F9J X-ray 2.10 A/B 42-655 [» ]
ProteinModelPortali P75906.
SMRi P75906. Positions 43-649.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-11513N.
STRINGi 511145.b1023.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74108 ; AAC74108 ; b1023 .
BAA35805 ; BAA35805 ; BAA35805 .
GeneIDi 12931056.
945604.
KEGGi ecj:Y75_p0995.
eco:b1023.
PATRICi 32117279. VBIEscCol129921_1063.

Organism-specific databases

EchoBASEi EB3624.
EcoGenei EG13864. pgaB.

Phylogenomic databases

eggNOGi COG0726.
HOGENOMi HOG000170240.
KOi K11931.
OMAi ELQTVDW.
OrthoDBi EOG6D8B8W.

Enzyme and pathway databases

BioCyci EcoCyc:G6530-MONOMER.
ECOL316407:JW5142-MONOMER.
MetaCyc:G6530-MONOMER.

Miscellaneous databases

PROi P75906.

Gene expression databases

Genevestigatori P75906.

Family and domain databases

Gene3Di 3.20.20.370. 1 hit.
InterProi IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR023854. PGA_deacetylase_PgaB.
IPR002509. Polysac_deacetylase.
[Graphical view ]
Pfami PF01522. Polysacc_deac_1. 1 hit.
[Graphical view ]
SUPFAMi SSF88713. SSF88713. 2 hits.
TIGRFAMsi TIGR03938. deacetyl_PgaB. 1 hit.
PROSITEi PS51677. NODB. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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], 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.

Entry informationi

Entry nameiPGAB_ECOLI
AccessioniPrimary (citable) accession number: P75906
Secondary accession number(s): Q9R7P5, Q9R7P7, Q9R7P8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 14, 2014
This is version 111 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

External Data

Dasty 3

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