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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

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

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 1 Publication; Lipid-anchor 1 Publication; Periplasmic side 1 Publication

GO - Cellular componenti

  1. cell outer membrane Source: UniProtKB-KW
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 – 2020PROSITE-ProRule annotationAdd
BLAST
Chaini21 – 672652Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylasePRO_0000024844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi21 – 211N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi21 – 211S-diacylglycerol cysteinePROSITE-ProRule annotation

Keywords - PTMi

Lipoprotein, Palmitate

Expressioni

Gene expression databases

GenevestigatoriP75906.

Interactioni

Protein-protein interaction databases

DIPiDIP-11513N.
STRINGi511145.b1023.

Structurei

Secondary structure

1
672
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 547Combined sources
Beta strandi57 – 604Combined sources
Helixi64 – 663Combined sources
Beta strandi68 – 703Combined sources
Helixi71 – 8313Combined sources
Helixi91 – 988Combined sources
Beta strandi108 – 1158Combined sources
Helixi118 – 13114Combined sources
Beta strandi135 – 1395Combined sources
Helixi141 – 1444Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi157 – 1593Combined sources
Helixi161 – 1633Combined sources
Helixi167 – 1759Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi200 – 2023Combined sources
Helixi203 – 2053Combined sources
Turni211 – 2144Combined sources
Helixi219 – 24022Combined sources
Beta strandi247 – 2493Combined sources
Helixi251 – 2533Combined sources
Helixi257 – 2659Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi285 – 2873Combined sources
Helixi298 – 3069Combined sources
Turni307 – 3093Combined sources
Beta strandi315 – 3195Combined sources
Helixi321 – 3233Combined sources
Helixi329 – 34618Combined sources
Beta strandi349 – 3546Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi373 – 3753Combined sources
Helixi382 – 39211Combined sources
Beta strandi396 – 4016Combined sources
Helixi419 – 4213Combined sources
Helixi422 – 4265Combined sources
Helixi429 – 4335Combined sources
Helixi440 – 45415Combined sources
Beta strandi460 – 4645Combined sources
Helixi478 – 48710Combined sources
Helixi493 – 4975Combined sources
Helixi500 – 52930Combined sources
Beta strandi534 – 5396Combined sources
Helixi541 – 5455Combined sources
Helixi547 – 5526Combined sources
Helixi557 – 5637Combined sources
Beta strandi565 – 5706Combined sources
Turni573 – 5775Combined sources
Helixi580 – 5823Combined sources
Helixi583 – 59513Combined sources
Helixi600 – 6034Combined sources
Beta strandi604 – 6129Combined sources
Beta strandi615 – 6173Combined sources
Beta strandi619 – 6213Combined sources
Helixi624 – 63613Combined sources
Beta strandi642 – 6454Combined sources
Helixi649 – 6513Combined sources
Helixi656 – 6594Combined sources
Helixi660 – 6623Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VUSX-ray1.65A/B42-309[»]
4F9DX-ray1.90A/B42-655[»]
4F9JX-ray2.10A/B42-655[»]
4P7LX-ray1.80A310-672[»]
4P7NX-ray1.89A310-672[»]
4P7OX-ray1.48A/B310-672[»]
4P7QX-ray1.65A310-672[»]
4P7RX-ray1.80A310-672[»]
ProteinModelPortaliP75906.
SMRiP75906. Positions 43-668.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini107 – 349243NodB homologyPROSITE-ProRule annotationAdd
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

Belongs to the polysaccharide deacetylase family.Curated
Contains 1 NodB homology domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MLRNGNKYLL MLVSIIMLTA CISQSRTSFI PPQDRESLLA EQPWPHNGFV
60 70 80 90 100
AISWHNVEDE AADQRFMSVR TSALREQFAW LRENGYQPVS IAQIREAHRG
110 120 130 140 150
GKPLPEKAVV LTFDDGYQSF YTRVFPILQA FQWPAVWAPV GSWVDTPADK
160 170 180 190 200
QVKFGDELVD REYFATWQQV REVARSRLVE LASHTWNSHY GIQANATGSL
210 220 230 240 250
LPVYVNRAYF TDHARYETAA EYRERIRLDA VKMTEYLRTK VEVNPHVFVW
260 270 280 290 300
PYGEANGIAI EELKKLGYDM FFTLESGLAN ASQLDSIPRV LIANNPSLKE
310 320 330 340 350
FAQQIITVQE KSPQRIMHID LDYVYDENLQ QMDRNIDVLI QRVKDMQIST
360 370 380 390 400
VYLQAFADPD GDGLVKEVWF PNRLLPMKAD IFSRVAWQLR TRSGVNIYAW
410 420 430 440 450
MPVLSWDLDP TLTRVKYLPT GEKKAQIHPE QYHRLSPFDD RVRAQVGMLY
460 470 480 490 500
EDLAGHAAFD GILFHDDALL SDYEDASAPA ITAYQQAGFS GSLSEIRQNP
510 520 530 540 550
EQFKQWARFK SRALTDFTLE LSARVKAIRG PHIKTARNIF ALPVIQPESE
560 570 580 590 600
AWFAQNYADF LKSYDWTAIM AMPYLEGVAE KSADQWLIQL TNQIKNIPQA
610 620 630 640 650
KDKSILELQA QNWQKNGQHQ AISSQQLAHW MSLLQLNGVK NYGYYPDNFL
660 670
HNQPEIDLIR PEFSTAWYPK ND
Length:672
Mass (Da):77,413
Last modified:February 1, 1997 - v1
Checksum:i8B68D0FFB657F4F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4P7L X-ray 1.80 A 310-672 [» ]
4P7N X-ray 1.89 A 310-672 [» ]
4P7O X-ray 1.48 A/B 310-672 [» ]
4P7Q X-ray 1.65 A 310-672 [» ]
4P7R X-ray 1.80 A 310-672 [» ]
ProteinModelPortali P75906.
SMRi P75906. Positions 43-668.
ModBasei Search...
MobiDBi 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: November 26, 2014
This is version 114 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