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 24-JAN-2024, entry version 160. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 511145-b1023; -. DR EnsemblBacteria; AAC74108; AAC74108; b1023. 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 InParanoid; P75906; -. DR OMA; KVYAWMP; -. DR OrthoDB; 9814639at2; -. DR BioCyc; EcoCyc:G6530-MONOMER; -. DR BioCyc; MetaCyc:G6530-MONOMER; -. 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 CDD; cd10964; CE4_PgaB_5s; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1. 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 NCBIfam; TIGR03938; deacetyl_PgaB; 1. DR PANTHER; PTHR34216; -; 1. DR PANTHER; PTHR34216:SF7; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE; 1. DR Pfam; PF14883; GHL13; 1. DR Pfam; PF01522; Polysacc_deac_1; 1. DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 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 //