ICAC_STAEQ
ID ICAC_STAEQ Reviewed; 355 AA.
AC Q5HKP7; Q54068;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=SERP2296;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ROLE IN BIOFILM FORMATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=8809760; DOI=10.1111/j.1365-2958.1996.tb02548.x;
RA Heilmann C., Schweitzer O., Gerke C., Vanittanakom N., Mack D., Goetz F.;
RT "Molecular basis of intercellular adhesion in the biofilm-forming
RT Staphylococcus epidermidis.";
RL Mol. Microbiol. 20:1083-1091(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
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).
RN [3]
RP FUNCTION IN PIA SYNTHESIS.
RX PubMed=9660830; DOI=10.1074/jbc.273.29.18586;
RA Gerke C., Kraft A., Sussmuth R., Schweitzer O., Goetz F.;
RT "Characterization of the N-acetylglucosaminyltransferase activity involved
RT in the biosynthesis of the Staphylococcus epidermidis polysaccharide
RT intercellular adhesin.";
RL J. Biol. Chem. 273:18586-18593(1998).
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 (By similarity). Is
CC essential for long-chain PIA synthesis. {ECO:0000250,
CC ECO:0000269|PubMed:8809760, ECO:0000269|PubMed:9660830}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Complete loss of the intercellular adhesion
CC phenotype. {ECO:0000269|PubMed:8809760}.
CC -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR EMBL; U43366; AAC06119.1; -; Genomic_DNA.
DR EMBL; CP000029; AAW53185.1; -; Genomic_DNA.
DR PIR; S77610; S77610.
DR RefSeq; WP_002484505.1; NC_002976.3.
DR AlphaFoldDB; Q5HKP7; -.
DR STRING; 176279.SERP2296; -.
DR EnsemblBacteria; AAW53185; AAW53185; SERP2296.
DR KEGG; ser:SERP2296; -.
DR eggNOG; COG3936; Bacteria.
DR HOGENOM; CLU_064947_1_0_9; -.
DR OMA; YHFYFVP; -.
DR OrthoDB; 1979131at2; -.
DR Proteomes; UP000000531; 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 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..355
FT /note="Probable poly-beta-1,6-N-acetyl-D-glucosamine export
FT protein"
FT /id="PRO_0000208079"
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
