ICAC_STAEP
ID ICAC_STAEP Reviewed; 355 AA.
AC P69518; Q54068;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 59.
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;
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=97-337;
RA Li H., Wen Y.;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SE5;
RX PubMed=15096544; DOI=10.1099/jmm.0.05372-0;
RA Handke L.D., Conlon K.M., Slater S.R., Elbaruni S., Fitzpatrick F.,
RA Humphreys H., Giles W.P., Rupp M.E., Fey P.D., O'Gara J.P.;
RT "Genetic and phenotypic analysis of biofilm phenotypic variation in
RT multiple Staphylococcus epidermidis isolates.";
RL J. Med. Microbiol. 53:367-374(2004).
RN [3]
RP PROBABLE FUNCTION.
RC STRAIN=Clinical isolate 1457;
RX PubMed=15501828; DOI=10.1074/jbc.m411374200;
RA Vuong C., Kocianova S., Voyich J.M., Yao Y., Fischer E.R., DeLeo F.R.,
RA Otto M.;
RT "A crucial role for exopolysaccharide modification in bacterial biofilm
RT formation, immune evasion, and virulence.";
RL J. Biol. Chem. 279:54881-54886(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.
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; AY382582; AAQ88123.1; -; Genomic_DNA.
DR EMBL; AY138959; AAN17774.1; -; Genomic_DNA.
DR RefSeq; WP_002484505.1; NZ_WLUZ01000001.1.
DR AlphaFoldDB; P69518; -.
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..355
FT /note="Probable poly-beta-1,6-N-acetyl-D-glucosamine export
FT protein"
FT /id="PRO_0000208078"
FT TRANSMEM 13..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..96
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 355 AA; 42090 MW; 7C847887B91894E3 CRC64;
MKKNKLELVY LRAFICVIII VTHLLTQITL ENEQMSDSSL ILQYYIRNIF IFGTPSFIIL
SQLLTTLNYE SVTINYLFSR FKYIFIPYLL IGLFYSYSES LITASSFKKQ FIENVVLGQW
YGYFIIIIMQ FFVLSYIIYK INFRLFNSKI LLLLAFIVQQ SYLHYFLNND TFHQFMTHYY
PLSENTMILG WIFYFFLGGY IGYNYEKILS FLEKYLIIVI MLTLGAYVLF IAVSGSDYWN
VTSFTYTLTL YNSVMFFLLL GVCMHFKTML LNTIKAISAF SFFIYLLHPI ILDSLFAYTN
IFEDNTIVFL AISLLMILGI CIGVGMMLRE FYIFRFVIGK QPYKLQFDQY QPNWN
