PGAA_ECOLI
ID PGAA_ECOLI Reviewed; 807 AA.
AC P69434; P75907;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Poly-beta-1,6-N-acetyl-D-glucosamine export protein;
DE Short=PGA export protein;
DE Short=Poly-beta-1,6-GlcNAc export protein;
DE Flags: Precursor;
GN Name=pgaA; Synonyms=ycdS; OrderedLocusNames=b1024, JW1010;
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 FUNCTION IN PGA EXPORT, DOMAIN, SUBCELLULAR LOCATION, AND DISRUPTION
RP 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 [6]
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: Exports the biofilm adhesin polysaccharide poly-beta-1,6-N-
CC acetyl-D-glucosamine (PGA) across the outer membrane. The PGA
CC transported seems to be partially N-deacetylated since N-deacetylation
CC of PGA by PgaB is needed for PGA export through the PgaA porin.
CC -!- FUNCTION: Required for the synthesis of the beta-1,6-GlcNAc
CC polysaccharide (PGA or poly-GlcNAc) that seems to serve as a biofilm
CC adhesin.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:18359807}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:18359807}.
CC -!- INDUCTION: Levels of this protein are negatively controlled by the
CC second messenger ppGpp (at protein level) at a post-transcriptional
CC level. Increased levels of c-di-GMP lead to decreased levels of PgaA.
CC {ECO:0000269|PubMed:19460094}.
CC -!- DOMAIN: Contains a predicted C-terminal beta-barrel porin domain and a
CC N-terminal periplasmic superhelical domain containing tetratricopeptide
CC repeats, which may mediate protein-protein interactions, perhaps with
CC PgaB. {ECO:0000269|PubMed:18359807}.
CC -!- DISRUPTION PHENOTYPE: Deletion of pgaA does not prevent PGA synthesis
CC but does block its export. The synthesized PGA is retained in the
CC periplasm and accumulates at the cell poles. Disruption of the pga
CC operon causes severe and persistent defects in the biofilm formation
CC process. {ECO:0000269|PubMed:15090514, ECO:0000269|PubMed:18359807}.
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DR EMBL; U00096; AAC74109.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35806.1; -; Genomic_DNA.
DR PIR; F64844; F64844.
DR RefSeq; NP_415543.1; NC_000913.3.
DR RefSeq; WP_000287458.1; NZ_SSZK01000002.1.
DR PDB; 4Y25; X-ray; 2.82 A; A=511-807.
DR PDBsum; 4Y25; -.
DR AlphaFoldDB; P69434; -.
DR SMR; P69434; -.
DR BioGRID; 4263226; 121.
DR IntAct; P69434; 1.
DR STRING; 511145.b1024; -.
DR TCDB; 1.B.55.1.1; the poly acetyl glucosamine porin (pgaa) family.
DR PaxDb; P69434; -.
DR PRIDE; P69434; -.
DR EnsemblBacteria; AAC74109; AAC74109; b1024.
DR EnsemblBacteria; BAA35806; BAA35806; BAA35806.
DR GeneID; 945596; -.
DR KEGG; ecj:JW1010; -.
DR KEGG; eco:b1024; -.
DR PATRIC; fig|1411691.4.peg.1245; -.
DR EchoBASE; EB3625; -.
DR eggNOG; COG0457; Bacteria.
DR HOGENOM; CLU_018289_0_0_6; -.
DR OMA; WDKRPYD; -.
DR BioCyc; EcoCyc:G6531-MON; -.
DR BioCyc; MetaCyc:G6531-MON; -.
DR BRENDA; 3.1.1.58; 2026.
DR PRO; PR:P69434; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoCyc.
DR GO; GO:1901515; F:poly-beta-1,6-N-acetyl-D-glucosamine transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015159; F:polysaccharide transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015774; P:polysaccharide transport; IDA:EcoCyc.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR023870; PGA_export_porin_PgaA.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SMART; SM00028; TPR; 1.
DR SUPFAM; SSF48452; SSF48452; 2.
DR TIGRFAMs; TIGR03939; PGA_TPR_OMP; 1.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Membrane; Reference proteome; Repeat;
KW Signal; TPR repeat; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..807
FT /note="Poly-beta-1,6-N-acetyl-D-glucosamine export protein"
FT /id="PRO_0000035694"
FT REPEAT 98..131
FT /note="TPR 1"
FT REPEAT 165..198
FT /note="TPR 2"
FT REPEAT 279..311
FT /note="TPR 3"
FT STRAND 518..530
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 540..547
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 551..565
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 574..586
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 589..599
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 604..617
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 620..629
FT /evidence="ECO:0007829|PDB:4Y25"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 644..670
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 675..689
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 691..697
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 700..705
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 717..723
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 725..735
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 738..753
FT /evidence="ECO:0007829|PDB:4Y25"
FT TURN 754..756
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 757..772
FT /evidence="ECO:0007829|PDB:4Y25"
FT TURN 773..775
FT /evidence="ECO:0007829|PDB:4Y25"
FT STRAND 776..807
FT /evidence="ECO:0007829|PDB:4Y25"
SQ SEQUENCE 807 AA; 92207 MW; B20067C3D41723FD CRC64;
MYSSSRKRCP KTKWALKLLT AAFLAASPAA KSAVNNAYDA LIIEARKGNT QPALSWFALK
SALSNNQIAD WLQIALWAGQ DKQVITVYNR YRHQQLPARG YAAVAVAYRN LQQWQNSLTL
WQKALSLEPQ NKDYQRGQIL TLADAGHYDT ALVKLKQLNS GAPDKANLLA EAYIYKLAGR
HQDELRAMTE SLPENASTQQ YPTEYVQALR NNQLAAAIDD ANLTPDIRAD IHAELVRLSF
MPTRSESERY AIADRALAQY AALEILWHDN PDRTAQYQRI QVDHLGALLT RDRYKDVISH
YQRLKKTGQI IPPWGQYWVA SAYLKDHQPK KAQSIMTELF YHKETIAPDL SDEELADLFY
SHLESENYPG ALTVTQHTIN TSPPFLRLMG TPTSIPNDTW LQGHSFLSTV AKYSNDLPQA
EMTARELAYN APGNQGLRID YASVLQARGW PRAAENELKK AEVIEPRNIN LEVEQAWTAL
TLQEWQQAAV LTHDVVEREP QDPGVVRLKR AVDVHNLAEL RIAGSTGIDA EGPDSGKHDV
DLTTIVYSPP LKDNWRGFAG FGYADGQFSE GKGIVRDWLA GVEWRSRNIW LEAEYAERVF
NHEHKPGARL SGWYDFNDNW RIGSQLERLS HRVPLRAMKN GVTGNSAQAY VRWYQNERRK
YGVSWAFTDF SDSNQRHEVS LEGQERIWSS PYLIVDFLPS LYYEQNTEHD TPYYNPIKTF
DIVPAFEASH LLWRSYENSW EQIFSAGVGA SWQKHYGTDV VTQLGYGQRI SWNDVIDAGA
TLRWEKRPYD GDREHNLYVE FDMTFRF
