ICAB_STAAC
ID ICAB_STAAC Reviewed; 292 AA.
AC Q5HCM9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, 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=SACOL2691;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
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. 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 -!- MISCELLANEOUS: In strain COL, the gene icaC is interrupted by a natural
CC frameshift.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; CP000046; AAW37341.1; -; Genomic_DNA.
DR RefSeq; WP_000877318.1; NC_002951.2.
DR AlphaFoldDB; Q5HCM9; -.
DR SMR; Q5HCM9; -.
DR EnsemblBacteria; AAW37341; AAW37341; SACOL2691.
DR KEGG; sac:SACOL2691; -.
DR HOGENOM; CLU_030024_3_2_9; -.
DR OMA; TYWHPNF; -.
DR Proteomes; UP000000530; 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..292
FT /note="Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase"
FT /id="PRO_0000024834"
FT DOMAIN 114..292
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
SQ SEQUENCE 292 AA; 34336 MW; 42E886D1B0DA47C7 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 ET
