ID   ICAB_STAAN              Reviewed;         290 AA.
AC   Q7A349;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=SA2461;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000018; BAB43766.1; -; Genomic_DNA.
DR   PIR; D90075; D90075.
DR   RefSeq; WP_000877369.1; NC_002745.2.
DR   AlphaFoldDB; Q7A349; -.
DR   SMR; Q7A349; -.
DR   EnsemblBacteria; BAB43766; BAB43766; BAB43766.
DR   KEGG; sau:SA2461; -.
DR   HOGENOM; CLU_030024_3_2_9; -.
DR   OMA; TYWHPNF; -.
DR   Proteomes; UP000000751; 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_0000024836"
FT   DOMAIN          114..290
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
SQ   SEQUENCE   290 AA;  34071 MW;  70F7F2B8454F2E2A CRC64;
     MKYRKLIILV 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