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ICAA_STAEQ
ID   ICAA_STAEQ              Reviewed;         412 AA.
AC   Q5HKQ0; Q54066;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Poly-beta-1,6-N-acetyl-D-glucosamine synthase;
DE            Short=PNAG synthase;
DE            Short=Poly-beta-1,6-GlcNAc synthase;
DE            EC=2.4.1.-;
DE   AltName: Full=Biofilm polysaccharide intercellular adhesin synthesis protein IcaA;
DE            Short=Biofilm PIA synthesis protein IcaA;
DE   AltName: Full=Intercellular adhesion protein A;
DE   AltName: Full=N-acetylglucosaminyltransferase IcaA;
GN   Name=icaA; OrderedLocusNames=SERP2293;
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, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
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: N-acetylglucosaminyltransferase that catalyzes the
CC       polymerization of single monomer units of UDP-N-acetylglucosamine to
CC       produce the linear homomer poly-beta-1,6-N-acetyl-D-glucosamine (PNAG,
CC       also referred to as PIA), a biofilm adhesin polysaccharide. Requires
CC       IcaD for full activity. {ECO:0000269|PubMed:8809760,
CC       ECO:0000269|PubMed:9660830}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9660830};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:9660830}.
CC   -!- DISRUPTION PHENOTYPE: Complete loss of the intercellular adhesion
CC       phenotype. {ECO:0000269|PubMed:8809760}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; U43366; AAC06117.1; -; Genomic_DNA.
DR   EMBL; CP000029; AAW53175.1; -; Genomic_DNA.
DR   PIR; S77608; S77608.
DR   RefSeq; WP_002497699.1; NC_002976.3.
DR   AlphaFoldDB; Q5HKQ0; -.
DR   SMR; Q5HKQ0; -.
DR   STRING; 176279.SERP2293; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   TCDB; 4.D.1.1.2; the putative vectorial glycosyl polymerization (vgp) family.
DR   EnsemblBacteria; AAW53175; AAW53175; SERP2293.
DR   KEGG; ser:SERP2293; -.
DR   eggNOG; COG1215; Bacteria.
DR   HOGENOM; CLU_023978_0_1_9; -.
DR   OMA; RNRWAEG; -.
DR   OrthoDB; 724641at2; -.
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:0008375; F:acetylglucosaminyltransferase activity; IEA:InterPro.
DR   GO; GO:0043708; P:cell adhesion involved in biofilm formation; IEA:InterPro.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR023853; PGA_PgaC/IcaA.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03937; PgaC_IcaA; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..412
FT                   /note="Poly-beta-1,6-N-acetyl-D-glucosamine synthase"
FT                   /id="PRO_0000059283"
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   412 AA;  47750 MW;  1E0F47E3081F7F06 CRC64;
     MHVFNFLLFY PIFMSIYWIV GSIYYFFIKE KPFNRSLLVK SEHQQVEGIS FLLACYNESE
     TVQDTLSSVL SLEYPEKEII IINDGSSDNT AEIIYDFKKN HDFKFVDLEV NRGKANALNE
     GIKQASYEYV MCLDADTVID DDAPFYMIED FKKNPKLGAV TGNPRIRNKS SILGKIQTIE
     YASIIGCIKR SQSLAGAINT ISGVFTLFKK SALKDVGYWD TDMITEDIAV SWKLHLFDYE
     IKYEPRALCW MLVPETIGGL WKQRVRWAQG GHEVLLRDFW PTIKTKKLSL YILMFEQIAS
     ITWVYIVLCY LSFLVITANI LDYTYLKYSF SIFFFSSFTM TFINIIQFTV ALFIDSRYEK
     KNIVGLIFLS WYPTLYWVIN AAVVIMAFPK ALKRKKGGYA TWSSPDRGNI QR
 
 
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