ID   ICAB_STAEQ              Reviewed;         289 AA.
AC   Q5HKP8; Q54067;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
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; OrderedLocusNames=SERP2295;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ROLE IN BIOFILM FORMATION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=8809760; DOI=10.1111/j.1365-2958.1996.tb02548.x;
RA   Heilmann C., Schweitzer O., Gerke C., Vanittanakom N., Mack D., Goetz F.;
RT   "Molecular basis of intercellular adhesion in the biofilm-forming
RT   Staphylococcus epidermidis.";
RL   Mol. Microbiol. 20:1083-1091(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Note=Attached to the cell
CC       surface. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Complete loss of the intercellular adhesion
CC       phenotype. {ECO:0000269|PubMed:8809760}.
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; U43366; AAC06118.1; -; Genomic_DNA.
DR   EMBL; CP000029; AAW53184.1; -; Genomic_DNA.
DR   PIR; S77609; S77609.
DR   RefSeq; WP_002484506.1; NC_002976.3.
DR   AlphaFoldDB; Q5HKP8; -.
DR   SMR; Q5HKP8; -.
DR   STRING; 176279.SERP2295; -.
DR   EnsemblBacteria; AAW53184; AAW53184; SERP2295.
DR   KEGG; ser:SERP2295; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_030024_3_2_9; -.
DR   OMA; TYWHPNF; -.
DR   OrthoDB; 635734at2; -.
DR   Proteomes; UP000000531; Chromosome.
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   3: Inferred from homology;
KW   Cell wall; Hydrolase; Reference proteome; 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_0000024841"
FT   DOMAIN          113..289
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
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