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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: 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

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • macromolecule deacylation Source: EcoCyc
  • single-species biofilm formation Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:G6530-MONOMER.
ECOL316407:JW5142-MONOMER.
MetaCyc:G6530-MONOMER.
BRENDAi3.1.1.58. 2026.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13864. pgaB.

Subcellular locationi

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Mutagenesisi115D → A: High decrease in catalytic activity. Unable to support biofilm formation and PGA secretion. 1 Publication1
Mutagenesisi184H → A: Unable to support biofilm formation and PGA secretion. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20PROSITE-ProRule annotationAdd BLAST20
ChainiPRO_000002484421 – 672Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylaseAdd BLAST652

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi21N-palmitoyl cysteinePROSITE-ProRule annotation1
Lipidationi21S-diacylglycerol cysteinePROSITE-ProRule annotation1

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

PaxDbiP75906.
PRIDEiP75906.

Interactioni

Protein-protein interaction databases

BioGridi4260050. 16 interactors.
DIPiDIP-11513N.
STRINGi511145.b1023.

Chemistry databases

BindingDBiP75906.

Structurei

Secondary structure

1672
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi48 – 54Combined sources7
Beta strandi57 – 60Combined sources4
Helixi64 – 66Combined sources3
Beta strandi68 – 70Combined sources3
Helixi71 – 83Combined sources13
Helixi91 – 98Combined sources8
Beta strandi108 – 115Combined sources8
Helixi118 – 131Combined sources14
Beta strandi135 – 139Combined sources5
Helixi141 – 144Combined sources4
Beta strandi148 – 150Combined sources3
Beta strandi152 – 154Combined sources3
Beta strandi157 – 159Combined sources3
Helixi161 – 163Combined sources3
Helixi167 – 175Combined sources9
Beta strandi178 – 181Combined sources4
Beta strandi190 – 193Combined sources4
Beta strandi200 – 202Combined sources3
Helixi203 – 205Combined sources3
Turni211 – 214Combined sources4
Helixi219 – 240Combined sources22
Beta strandi247 – 249Combined sources3
Helixi251 – 253Combined sources3
Helixi257 – 265Combined sources9
Beta strandi270 – 272Combined sources3
Beta strandi285 – 287Combined sources3
Helixi298 – 306Combined sources9
Turni307 – 309Combined sources3
Beta strandi315 – 319Combined sources5
Helixi321 – 323Combined sources3
Helixi329 – 346Combined sources18
Beta strandi349 – 354Combined sources6
Beta strandi368 – 370Combined sources3
Beta strandi373 – 375Combined sources3
Helixi382 – 392Combined sources11
Beta strandi396 – 401Combined sources6
Helixi419 – 421Combined sources3
Helixi422 – 426Combined sources5
Helixi429 – 433Combined sources5
Helixi440 – 454Combined sources15
Beta strandi460 – 464Combined sources5
Helixi478 – 487Combined sources10
Helixi493 – 497Combined sources5
Helixi500 – 529Combined sources30
Beta strandi534 – 539Combined sources6
Helixi541 – 545Combined sources5
Helixi547 – 552Combined sources6
Helixi557 – 563Combined sources7
Beta strandi565 – 570Combined sources6
Turni573 – 577Combined sources5
Helixi580 – 582Combined sources3
Helixi583 – 595Combined sources13
Helixi600 – 603Combined sources4
Beta strandi604 – 612Combined sources9
Beta strandi615 – 617Combined sources3
Beta strandi619 – 621Combined sources3
Helixi624 – 636Combined sources13
Beta strandi642 – 645Combined sources4
Helixi649 – 651Combined sources3
Helixi656 – 659Combined sources4
Helixi660 – 662Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini107 – 349NodB homologyPROSITE-ProRule annotationAdd BLAST243

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

eggNOGiENOG4107BJW. Bacteria.
COG0726. LUCA.
HOGENOMiHOG000170240.
KOiK11931.
OMAiKVYAWMP.

Family and domain databases

Gene3Di3.20.20.370. 1 hit.
InterProiIPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. NODB_dom.
IPR023854. PGA_deacetylase_PgaB.
IPR032772. PGA_deacetylase_PgaB_C.
[Graphical view]
PfamiPF14883. GHL13. 1 hit.
PF01522. 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.
WP_000945561.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74108; AAC74108; b1023.
BAA35805; BAA35805; BAA35805.
GeneIDi945604.
KEGGiecj:JW5142.
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.
PIRiE64844.
RefSeqiNP_415542.1. NC_000913.3.
WP_000945561.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260050. 16 interactors.
DIPiDIP-11513N.
STRINGi511145.b1023.

Chemistry databases

BindingDBiP75906.

Proteomic databases

PaxDbiP75906.
PRIDEiP75906.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74108; AAC74108; b1023.
BAA35805; BAA35805; BAA35805.
GeneIDi945604.
KEGGiecj:JW5142.
eco:b1023.
PATRICi32117279. VBIEscCol129921_1063.

Organism-specific databases

EchoBASEiEB3624.
EcoGeneiEG13864. pgaB.

Phylogenomic databases

eggNOGiENOG4107BJW. Bacteria.
COG0726. LUCA.
HOGENOMiHOG000170240.
KOiK11931.
OMAiKVYAWMP.

Enzyme and pathway databases

BioCyciEcoCyc:G6530-MONOMER.
ECOL316407:JW5142-MONOMER.
MetaCyc:G6530-MONOMER.
BRENDAi3.1.1.58. 2026.

Miscellaneous databases

PROiP75906.

Family and domain databases

Gene3Di3.20.20.370. 1 hit.
InterProiIPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR002509. NODB_dom.
IPR023854. PGA_deacetylase_PgaB.
IPR032772. PGA_deacetylase_PgaB_C.
[Graphical view]
PfamiPF14883. GHL13. 1 hit.
PF01522. 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]
ProtoNetiSearch...

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 2, 2016
This is version 127 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.