PGAD_ECOLI
ID PGAD_ECOLI Reviewed; 137 AA.
AC P69432; P75904;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Biofilm PGA synthesis protein PgaD;
GN Name=pgaD; Synonyms=ycdP; OrderedLocusNames=b1021, JW1006;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP ROLE IN THE SYNTHESIS OF A BIOFILM POLYSACCHARIDE, OPERON STRUCTURE, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15090514; DOI=10.1128/jb.186.9.2724-2734.2004;
RA Wang X., Preston J.F. III, Romeo T.;
RT "The pgaABCD locus of Escherichia coli promotes the synthesis of a
RT polysaccharide adhesin required for biofilm formation.";
RL J. Bacteriol. 186:2724-2734(2004).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP FUNCTION IN PGA SYNTHESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18359807; DOI=10.1128/jb.01920-07;
RA Itoh Y., Rice J.D., Goller C., Pannuri A., Taylor J., Meisner J.,
RA Beveridge T.J., Preston J.F. III, Romeo T.;
RT "Roles of pgaABCD genes in synthesis, modification, and export of the
RT Escherichia coli biofilm adhesin poly-beta-1,6-N-acetyl-D-glucosamine.";
RL J. Bacteriol. 190:3670-3680(2008).
RN [7]
RP ROLE IN BIOFILM FORMATION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / AB400;
RX PubMed=19460094; DOI=10.1111/j.1365-2958.2009.06739.x;
RA Boehm A., Steiner S., Zaehringer F., Casanova A., Hamburger F., Ritz D.,
RA Keck W., Ackermann M., Schirmer T., Jenal U.;
RT "Second messenger signalling governs Escherichia coli biofilm induction
RT upon ribosomal stress.";
RL Mol. Microbiol. 72:1500-1516(2009).
CC -!- FUNCTION: Required for the synthesis of poly-beta-1,6-N-acetyl-D-
CC glucosamine (PGA), a biofilm adhesin polysaccharide. May assist the
CC glycosyltransferase PgaC in the polymerization of PGA.
CC {ECO:0000269|PubMed:15090514, ECO:0000269|PubMed:18359807,
CC ECO:0000269|PubMed:19460094}.
CC -!- INTERACTION:
CC P69432; P25522: mnmE; NbExp=5; IntAct=EBI-562069, EBI-550986;
CC P69432; P75905: pgaC; NbExp=2; IntAct=EBI-562069, EBI-561450;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: Levels of this protein are positively controlled by the
CC second messenger c-di-GMP (at protein level) at a post-transcriptional
CC level. Increased levels of c-di-GMP lead to increased levels of PgaD.
CC {ECO:0000269|PubMed:19460094}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not synthesize PGA.
CC {ECO:0000269|PubMed:15090514, ECO:0000269|PubMed:18359807}.
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DR EMBL; U00096; AAC74106.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35802.1; -; Genomic_DNA.
DR PIR; C64844; C64844.
DR RefSeq; NP_415540.1; NC_000913.3.
DR RefSeq; WP_001061095.1; NZ_STEB01000006.1.
DR AlphaFoldDB; P69432; -.
DR BioGRID; 4260055; 21.
DR BioGRID; 851820; 7.
DR ComplexPortal; CPX-3743; pgaCD beta-glycosyltransferase complex.
DR DIP; DIP-48114N; -.
DR IntAct; P69432; 7.
DR MINT; P69432; -.
DR STRING; 511145.b1021; -.
DR PaxDb; P69432; -.
DR PRIDE; P69432; -.
DR DNASU; 947503; -.
DR EnsemblBacteria; AAC74106; AAC74106; b1021.
DR EnsemblBacteria; BAA35802; BAA35802; BAA35802.
DR GeneID; 58391625; -.
DR GeneID; 947503; -.
DR KEGG; ecj:JW1006; -.
DR KEGG; eco:b1021; -.
DR PATRIC; fig|1411691.4.peg.1248; -.
DR EchoBASE; EB3622; -.
DR eggNOG; COG3658; Bacteria.
DR eggNOG; ENOG50338G7; Bacteria.
DR HOGENOM; CLU_131509_0_0_6; -.
DR OMA; VFWESEA; -.
DR BioCyc; EcoCyc:G6528-MON; -.
DR BioCyc; MetaCyc:G6528-MON; -.
DR PRO; PR:P69432; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0043708; P:cell adhesion involved in biofilm formation; IDA:ComplexPortal.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IEA:InterPro.
DR InterPro; IPR023829; PGA_PgaD.
DR Pfam; PF13994; PgaD; 1.
DR TIGRFAMs; TIGR03940; PGA_PgaD; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..137
FT /note="Biofilm PGA synthesis protein PgaD"
FT /id="PRO_0000058349"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..53
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 137 AA; 16082 MW; 574776B68F667D5D CRC64;
MNNLIITTRQ SPVRLLVDYV ATTILWTLFA LFIFLFAMDL LTGYYWQSEA RSRLQFYFLL
AVANAVVLIV WALYNKLRFQ KQQHHAAYQY TPQEYAESLA IPDELYQQLQ KSHRMSVHFT
SQGQIKMVVS EKALVRA
