ID   ICAB_STAAW              Reviewed;         290 AA.
AC   Q8NUI6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=MW2588;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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. N-deacetylation is crucial for attachment of the
CC       polysaccharide to the bacterial cell surface; it leads to the
CC       introduction of positive charges in the otherwise neutral PIA polymer,
CC       allowing electrostatic interactions (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Note=Attached to the cell
CC       surface. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000033; BAB96453.1; -; Genomic_DNA.
DR   RefSeq; WP_000877317.1; NC_003923.1.
DR   AlphaFoldDB; Q8NUI6; -.
DR   SMR; Q8NUI6; -.
DR   EnsemblBacteria; BAB96453; BAB96453; BAB96453.
DR   KEGG; sam:MW2588; -.
DR   HOGENOM; CLU_030024_3_2_9; -.
DR   OMA; TYWHPNF; -.
DR   Proteomes; UP000000418; 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; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..290
FT                   /note="Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase"
FT                   /id="PRO_0000024839"
FT   DOMAIN          114..290
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
SQ   SEQUENCE   290 AA;  34105 MW;  76D1B0DA47C726A8 CRC64;
     MKYRKFIILV LSILIILPVS TLDGHHIANA DDDSPKKLKY KENSALALNY HRVRKANFLN
     NFIYFFSSSK EIKNYSVSQS QFESQIKWLK SHDAKFLTLK EFLYYKKKGK FPKRSVWINF
     DDMDETIYEN AYPILKKYKI PATGFIITGH VGEENFHNLD MISKKELKEM YKTGLWEFET
     HTHDLHNLSK NNKSKLMKAS EATIIKDLNK SEKYLTKNFK KSQKTIAYPY GLMNDDKLPV
     IKKAGLKYGF SLEEKAVTPN SNDYYIPRIL ISDDAFEHLI KRWDGFHEKD