ICAB_STAAM
ID ICAB_STAAM Reviewed; 290 AA.
AC Q99QX2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=SAV2668;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
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; BA000017; BAB58830.1; -; Genomic_DNA.
DR RefSeq; WP_000877369.1; NC_002758.2.
DR AlphaFoldDB; Q99QX2; -.
DR SMR; Q99QX2; -.
DR PaxDb; Q99QX2; -.
DR EnsemblBacteria; BAB58830; BAB58830; SAV2668.
DR KEGG; sav:SAV2668; -.
DR HOGENOM; CLU_030024_3_2_9; -.
DR OMA; TYWHPNF; -.
DR PhylomeDB; Q99QX2; -.
DR BioCyc; SAUR158878:SAV_RS14570-MON; -.
DR Proteomes; UP000002481; 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_0000024835"
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
