ICAB_STAAS
ID ICAB_STAAS Reviewed; 290 AA.
AC Q6G606;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=SAS2554;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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. 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}.
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; BX571857; CAG44371.1; -; Genomic_DNA.
DR RefSeq; WP_000877317.1; NC_002953.3.
DR AlphaFoldDB; Q6G606; -.
DR SMR; Q6G606; -.
DR KEGG; sas:SAS2554; -.
DR HOGENOM; CLU_030024_3_2_9; -.
DR OMA; TYWHPNF; -.
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_0000024838"
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
