PGAB_ECOLI
ID PGAB_ECOLI Reviewed; 672 AA.
AC P75906; Q9R7P5; Q9R7P7; Q9R7P8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase;
DE Short=PGA N-deacetylase;
DE Short=Poly-beta-1,6-GlcNAc N-deacetylase;
DE EC=3.5.1.-;
DE Flags: Precursor;
GN Name=pgaB; Synonyms=ycdR; OrderedLocusNames=b1023, JW5142;
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], AND SEQUENCE REVISION.
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 AS A PGA DEACETYLASE, MUTAGENESIS OF ASP-115 AND HIS-184, DOMAIN,
RP SUBCELLULAR LOCATION, 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).
CC -!- FUNCTION: Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-
CC glucosamine (PGA), a biofilm adhesin polysaccharide. N-deacetylation
CC promotes PGA export through the PgaA porin.
CC {ECO:0000269|PubMed:15090514, ECO:0000269|PubMed:18359807}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:18359807}; Lipid-anchor
CC {ECO:0000305|PubMed:18359807}; Periplasmic side
CC {ECO:0000305|PubMed:18359807}.
CC -!- DOMAIN: Contains a N-terminal polysaccharide deacetylase domain, and a
CC C-terminal domain required for PGA N-deacetylation that may be involved
CC in binding to unmodified poly-beta-1,6-GlcNAc and thereby assists
CC catalysis by the deacetylase domain. {ECO:0000269|PubMed:18359807}.
CC -!- DISRUPTION PHENOTYPE: Deletion of pgaB does not prevent PGA synthesis
CC but does block its export and biofilm formation. The synthesized PGA is
CC retained in the periplasm and accumulates at the cell poles.
CC {ECO:0000269|PubMed:15090514, ECO:0000269|PubMed:18359807}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74108.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35805.2; -; Genomic_DNA.
DR PIR; E64844; E64844.
DR RefSeq; NP_415542.1; NC_000913.3.
DR RefSeq; WP_000945561.1; NZ_STEB01000006.1.
DR PDB; 3VUS; X-ray; 1.65 A; A/B=42-309.
DR PDB; 4F9D; X-ray; 1.90 A; A/B=42-655.
DR PDB; 4F9J; X-ray; 2.10 A; A/B=42-655.
DR PDB; 4P7L; X-ray; 1.80 A; A=310-672.
DR PDB; 4P7N; X-ray; 1.89 A; A=310-672.
DR PDB; 4P7O; X-ray; 1.48 A; A/B=310-672.
DR PDB; 4P7Q; X-ray; 1.65 A; A=310-672.
DR PDB; 4P7R; X-ray; 1.80 A; A=310-672.
DR PDBsum; 3VUS; -.
DR PDBsum; 4F9D; -.
DR PDBsum; 4F9J; -.
DR PDBsum; 4P7L; -.
DR PDBsum; 4P7N; -.
DR PDBsum; 4P7O; -.
DR PDBsum; 4P7Q; -.
DR PDBsum; 4P7R; -.
DR AlphaFoldDB; P75906; -.
DR SMR; P75906; -.
DR BioGRID; 4260050; 16.
DR DIP; DIP-11513N; -.
DR STRING; 511145.b1023; -.
DR BindingDB; P75906; -.
DR ChEMBL; CHEMBL4295582; -.
DR PaxDb; P75906; -.
DR PRIDE; P75906; -.
DR EnsemblBacteria; AAC74108; AAC74108; b1023.
DR EnsemblBacteria; BAA35805; BAA35805; BAA35805.
DR GeneID; 945604; -.
DR KEGG; ecj:JW5142; -.
DR KEGG; eco:b1023; -.
DR PATRIC; fig|1411691.4.peg.1246; -.
DR EchoBASE; EB3624; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG1649; Bacteria.
DR HOGENOM; CLU_030024_9_2_6; -.
DR OMA; KVYAWMP; -.
DR BioCyc; EcoCyc:G6530-MON; -.
DR BioCyc; MetaCyc:G6530-MON; -.
DR BRENDA; 3.1.1.58; 2026.
DR PRO; PR:P75906; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IDA:EcoCyc.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0043708; P:cell adhesion involved in biofilm formation; IEA:InterPro.
DR GO; GO:0098732; P:macromolecule deacylation; IDA:EcoCyc.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR023854; PGA_deacetylase_PgaB.
DR InterPro; IPR032772; PGA_deacetylase_PgaB_C.
DR Pfam; PF14883; GHL13; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR TIGRFAMs; TIGR03938; deacetyl_PgaB; 1.
DR PROSITE; PS51677; NODB; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..672
FT /note="Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase"
FT /id="PRO_0000024844"
FT DOMAIN 107..349
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 115
FT /note="D->A: High decrease in catalytic activity. Unable to
FT support biofilm formation and PGA secretion."
FT /evidence="ECO:0000269|PubMed:18359807"
FT MUTAGEN 184
FT /note="H->A: Unable to support biofilm formation and PGA
FT secretion."
FT /evidence="ECO:0000269|PubMed:18359807"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:3VUS"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4F9D"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:3VUS"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:3VUS"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3VUS"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3VUS"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3VUS"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:4F9D"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:4F9D"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3VUS"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:3VUS"
FT HELIX 219..240
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:3VUS"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3VUS"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3VUS"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3VUS"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:3VUS"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:4F9D"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 329..346
FT /evidence="ECO:0007829|PDB:4P7O"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:4P7O"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:4P7O"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 382..392
FT /evidence="ECO:0007829|PDB:4P7O"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:4F9D"
FT HELIX 422..426
FT /evidence="ECO:0007829|PDB:4F9D"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:4F9D"
FT HELIX 440..454
FT /evidence="ECO:0007829|PDB:4P7O"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 478..487
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 493..497
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 500..529
FT /evidence="ECO:0007829|PDB:4P7O"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 541..545
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 547..552
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 557..563
FT /evidence="ECO:0007829|PDB:4P7O"
FT STRAND 565..570
FT /evidence="ECO:0007829|PDB:4P7O"
FT TURN 573..577
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 583..595
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 600..603
FT /evidence="ECO:0007829|PDB:4P7O"
FT STRAND 604..612
FT /evidence="ECO:0007829|PDB:4P7O"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:4P7R"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:4P7L"
FT HELIX 624..636
FT /evidence="ECO:0007829|PDB:4P7O"
FT STRAND 642..645
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 656..659
FT /evidence="ECO:0007829|PDB:4P7O"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:4P7O"
SQ SEQUENCE 672 AA; 77413 MW; 8B68D0FFB657F4F2 CRC64;
MLRNGNKYLL MLVSIIMLTA CISQSRTSFI PPQDRESLLA EQPWPHNGFV AISWHNVEDE
AADQRFMSVR TSALREQFAW LRENGYQPVS IAQIREAHRG GKPLPEKAVV LTFDDGYQSF
YTRVFPILQA FQWPAVWAPV GSWVDTPADK QVKFGDELVD REYFATWQQV REVARSRLVE
LASHTWNSHY GIQANATGSL LPVYVNRAYF TDHARYETAA EYRERIRLDA VKMTEYLRTK
VEVNPHVFVW PYGEANGIAI EELKKLGYDM FFTLESGLAN ASQLDSIPRV LIANNPSLKE
FAQQIITVQE KSPQRIMHID LDYVYDENLQ QMDRNIDVLI QRVKDMQIST VYLQAFADPD
GDGLVKEVWF PNRLLPMKAD IFSRVAWQLR TRSGVNIYAW MPVLSWDLDP TLTRVKYLPT
GEKKAQIHPE QYHRLSPFDD RVRAQVGMLY EDLAGHAAFD GILFHDDALL SDYEDASAPA
ITAYQQAGFS GSLSEIRQNP EQFKQWARFK SRALTDFTLE LSARVKAIRG PHIKTARNIF
ALPVIQPESE AWFAQNYADF LKSYDWTAIM AMPYLEGVAE KSADQWLIQL TNQIKNIPQA
KDKSILELQA QNWQKNGQHQ AISSQQLAHW MSLLQLNGVK NYGYYPDNFL HNQPEIDLIR
PEFSTAWYPK ND
