ICAC_STAAR
ID ICAC_STAAR Reviewed; 350 AA.
AC Q6GDD5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Probable poly-beta-1,6-N-acetyl-D-glucosamine export protein;
DE Short=PGA export protein;
DE Short=Poly-beta-1,6-GlcNAc export protein;
DE AltName: Full=Biofilm polysaccharide intercellular adhesin export protein;
DE Short=Biofilm PIA export protein;
DE AltName: Full=Intercellular adhesion protein C;
GN Name=icaC; OrderedLocusNames=SAR2750;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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: Presumably involved in the export of the biofilm adhesin
CC polysaccharide poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also
CC referred to as PIA) across the cell membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR EMBL; BX571856; CAG41726.1; -; Genomic_DNA.
DR RefSeq; WP_000723844.1; NC_002952.2.
DR AlphaFoldDB; Q6GDD5; -.
DR KEGG; sar:SAR2750; -.
DR HOGENOM; CLU_064947_1_0_9; -.
DR OMA; YHFYFVP; -.
DR OrthoDB; 1979131at2; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..350
FT /note="Probable poly-beta-1,6-N-acetyl-D-glucosamine export
FT protein"
FT /id="PRO_0000208074"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..328
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 350 AA; 41358 MW; EDDB571FD3A0285E CRC64;
MKKIRLELVY LRAIICAIII VTHLLTQITL KHENMEGGSL VLQFYIRNIV IFGTPCFIIL
SQLLTTLNYQ KVTYRYLTTR VKYILIPYIL MGLFYSYSES LLTDTSFQKQ FIENVLLGQW
YGYFIVVIMQ FFILSYIIFK INYNLFNSKI LLLLSFILQQ SFLYYFTNNT AFHDTVLHYY
PLSENTIIFG WIFYFFLGAY MGYNYERVLN FLERYLVIMI VLAVATYFVF IALANGDYWN
VTSFSYSLTP YNSIMFIVIL GICTHFKTML FNTIQMISAF SFFIYLLHPI ILDSLFAYTN
IFEDNTMVFL AISLLFILGL CIGVGMILRE FYIFRFIIGK QPYKLNINAY