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P75906

- PGAB_ECOLI

UniProt

P75906 - PGAB_ECOLI

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
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    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

    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-SubCell

    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 – 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.
    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

    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...
    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

    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: October 1, 2014
    This is version 112 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