PGAB_ECO57
ID PGAB_ECO57 Reviewed; 672 AA.
AC Q8XAR3; Q7AFM2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
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; OrderedLocusNames=Z1525, ECs1269;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG55641.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34692.1; -; Genomic_DNA.
DR PIR; E85647; E85647.
DR PIR; E90787; E90787.
DR RefSeq; NP_309296.1; NC_002695.1.
DR RefSeq; WP_000945580.1; NZ_SEKU01000016.1.
DR AlphaFoldDB; Q8XAR3; -.
DR SMR; Q8XAR3; -.
DR STRING; 155864.EDL933_1450; -.
DR EnsemblBacteria; AAG55641; AAG55641; Z1525.
DR EnsemblBacteria; BAB34692; BAB34692; ECs_1269.
DR GeneID; 912831; -.
DR KEGG; ece:Z1525; -.
DR KEGG; ecs:ECs_1269; -.
DR PATRIC; fig|386585.9.peg.1377; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG1649; Bacteria.
DR HOGENOM; CLU_030024_9_2_6; -.
DR OMA; KVYAWMP; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0043708; P:cell adhesion involved in biofilm formation; IEA:InterPro.
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 3: Inferred from homology;
KW Cell outer membrane; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW 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_0000024845"
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"
SQ SEQUENCE 672 AA; 77426 MW; CC845FAF46194462 CRC64;
MLRNGNKYLL MLVSIIMLTA CISQSRTSFI PPQDRKSLLA EQPWPHNGFV AISWHNVEDE
AADQRFMSVR TSALREQFAW LRENGYQPVS IAQIREAHRG GKPLPEKAVV LTFDDGYQSF
YTRVFPILQA FQWPAVWAPV GSWVDTPADK QVKFGDELVD REYFATWQQV REVARSRLVE
LASHTWNSHY GIQANATGSL LPVYVNRAYF TDHARYETAA EYRERIRLDA VKMTEYLRTK
VEVNPHVFIW 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
