ICAB_STAEP
ID ICAB_STAEP Reviewed; 289 AA.
AC Q6TYB1; Q54067;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase;
DE Short=PNAG N-deacetylase;
DE Short=Poly-beta-1,6-GlcNAc N-deacetylase;
DE EC=3.5.1.-;
DE AltName: Full=Biofilm polysaccharide intercellular adhesin deacetylase;
DE Short=Biofilm PIA deacetylase;
DE AltName: Full=Intercellular adhesion protein B;
DE Flags: Precursor;
GN Name=icaB;
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=97-337;
RA Li H., Wen Y.;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SE5;
RX PubMed=15096544; DOI=10.1099/jmm.0.05372-0;
RA Handke L.D., Conlon K.M., Slater S.R., Elbaruni S., Fitzpatrick F.,
RA Humphreys H., Giles W.P., Rupp M.E., Fey P.D., O'Gara J.P.;
RT "Genetic and phenotypic analysis of biofilm phenotypic variation in
RT multiple Staphylococcus epidermidis isolates.";
RL J. Med. Microbiol. 53:367-374(2004).
RN [3]
RP FUNCTION AS A PIA DEACETYLASE, ROLE IN VIRULENCE, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Clinical isolate 1457;
RX PubMed=15501828; DOI=10.1074/jbc.m411374200;
RA Vuong C., Kocianova S., Voyich J.M., Yao Y., Fischer E.R., DeLeo F.R.,
RA Otto M.;
RT "A crucial role for exopolysaccharide modification in bacterial biofilm
RT formation, immune evasion, and virulence.";
RL J. Biol. Chem. 279:54881-54886(2004).
CC -!- FUNCTION: Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-
CC glucosamine (PNAG, also referred to as PIA), a biofilm adhesin
CC polysaccharide. In fact, the IcaB deacetylase converts 15 to 20% of the
CC GlcNAc residues of PNAG to glucosamine. N-deacetylation is crucial for
CC attachment of the polysaccharide to the bacterial cell surface; it
CC leads to the introduction of positive charges in the otherwise neutral
CC PIA polymer, allowing electrostatic interactions. Deacetylation of the
CC polymer is also essential for key virulence mechanisms of
CC S.epidermidis, namely biofilm formation, colonization, and resistance
CC to neutrophil phagocytosis and human antibacterial peptides.
CC {ECO:0000269|PubMed:15501828}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:15501828}. Note=Attached to the cell surface.
CC -!- DISRUPTION PHENOTYPE: Deletion of icaB leads to shedding of the PIA
CC polymer from the cell surface to the culture filtrate, and an inability
CC to support biofilm formation. Deacetylated PIA is not observed in the
CC mutant strains. Furthermore, these strains are unable to form biofilms,
CC show significantly higher sensitivity to the effects of antibacterial
CC peptides, their adhesion to epithelial cells is significantly lower
CC than that of the wild-type, their phagocytosis by human neutrophils is
CC highly increased, and their persistence is significantly impaired in a
CC murine model of device-related infection.
CC {ECO:0000269|PubMed:15501828}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; AY382582; AAQ88122.1; -; Genomic_DNA.
DR EMBL; AY138959; AAN17773.1; -; Genomic_DNA.
DR RefSeq; WP_002484506.1; NZ_WLUZ01000001.1.
DR AlphaFoldDB; Q6TYB1; -.
DR SMR; Q6TYB1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR023872; PNAG_deacetylase.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR TIGRFAMs; TIGR03933; PIA_icaB; 1.
DR PROSITE; PS51677; NODB; 1.
PE 1: Evidence at protein level;
KW Cell wall; Hydrolase; Secreted; Signal; Virulence.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..289
FT /note="Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase"
FT /id="PRO_0000024840"
FT DOMAIN 113..289
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT VARIANT 131
FT /note="F -> S (in strain: 97-337)"
FT VARIANT 236
FT /note="K -> R (in strain: 97-337)"
SQ SEQUENCE 289 AA; 33636 MW; BED61A9BC151CE3E CRC64;
MKPFKLIFIS ALMILIMTNA TPISHLNAQA NEENKKLKYE KNSALALNYH RVRKKDPLND
FISLLSGSKE IKNYSVTDQE FKSQIQWLKA HDAKFLTLKE FIKYKEKGKF PKRSVWINFD
DMDQTIYDNA FPVLKKYHIP ATGFLITNHI GSTNFHNLNL LSKKQLDEMY ETGLWDFESH
THDLHALKKG NKSKFLDSSQ SVASKDIKKS EHYLNKNYPK NERALAYPYG LINDDKIKAM
KKNGIQYGFT LQEKAVTPDA DNYRIPRILV SNDAFETLIK EWDGFDEEK
