ID   WEFF_STRMT              Reviewed;         333 AA.
AC   Q6L5Q5;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Receptor polysaccharide phosphotransferase WefF;
DE            EC=2.7.-.-;
DE   AltName: Full=Stealth protein WefF;
GN   Name=wefF;
OS   Streptococcus mitis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=28037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE EXCHANGE WITH WEFC OF
RP   S.GORDONII.
RC   STRAIN=J22;
RX   PubMed=16164562; DOI=10.1111/j.1365-2958.2005.04820.x;
RA   Yoshida Y., Ganguly S., Bush C.A., Cisar J.O.;
RT   "Carbohydrate engineering of the recognition motifs in streptococcal co-
RT   aggregation receptor polysaccharides.";
RL   Mol. Microbiol. 58:244-256(2005).
RN   [2]
RP   IDENTIFICATION AS A STEALTH PROTEIN, AND PREDICTION OF FUNCTION.
RX   PubMed=16299590; DOI=10.1371/journal.pcbi.0010063;
RA   Sperisen P., Schmid C.D., Bucher P., Zilian O.;
RT   "Stealth proteins: in silico identification of a novel protein family
RT   rendering bacterial pathogens invisible to host immune defense.";
RL   PLoS Comput. Biol. 1:492-499(2005).
CC   -!- FUNCTION: Part of the type 2G receptor polysaccharide (RPS)
CC       biosynthesis locus. Essential for cell surface RPS production, and the
CC       host-like Gal beta 1-3GalNAc (G) motif of the RPS. Probably encodes a
CC       1-3GalNAc alpha transferase.
CC   -!- MISCELLANEOUS: The cell wall polysaccharides of some oral streptococci
CC       act as receptors for the lectin-like surface adhesins on other members
CC       of the oral biofilm community, especially type 2 fimbriated strains of
CC       Actinomyces naeslundii, allowing colonization of the human tooth
CC       surface. Recognition of these receptor polysaccharides (RPS) depends on
CC       the presence of a host-like motif, either GalNAc beta 1-3Gal (Gn) or
CC       Gal beta 1-3GalNAc (G), within the oligosaccharide repeating units of
CC       different RPS structural types. Type 2Gn RPS of S.gordonii strain 38
CC       and type 2G RPS of S.mitis strain J22 are composed of heptasaccharide
CC       repeats that are identical except for their host-like motifs. This
CC       mimicry of the host glycoconjugates may help the bacteria evade the
CC       immune system.
CC   -!- MISCELLANEOUS: Stealth proteins are part of a protein family that is
CC       conserved from bacteria to higher eukaryotes. Family members were first
CC       identified in microbes as proteins that help pathogens to elude the
CC       host innate immune system. Microbial stealth proteins are involved in
CC       the biosynthesis of exopolysaccharides. Stealth proteins are predicted
CC       to function as hexose-1-phosphoryltransferases.
CC   -!- SIMILARITY: Belongs to the stealth family. {ECO:0000305}.
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DR   EMBL; AB181235; BAD22643.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6L5Q5; -.
DR   GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR031358; Stealth_CR1.
DR   InterPro; IPR021520; Stealth_CR2.
DR   InterPro; IPR031357; Stealth_CR3.
DR   Pfam; PF17101; Stealth_CR1; 1.
DR   Pfam; PF11380; Stealth_CR2; 1.
DR   Pfam; PF17102; Stealth_CR3; 1.
PE   3: Inferred from homology;
KW   Exopolysaccharide synthesis; Transferase.
FT   CHAIN           1..333
FT                   /note="Receptor polysaccharide phosphotransferase WefF"
FT                   /id="PRO_0000235965"
SQ   SEQUENCE   333 AA;  38522 MW;  15D9DB0F3A447B97 CRC64;
     MVEKIDFVVA WVDGNDPVWR KKKAQYDGTI NTSKEGMNSD KAYREWGTFK YWFRGVEKFA
     PWVNKVYLVT DNQKPSWLEL NSDKLVLVDH TEIICNDYLP VFSANPIESN IHRIPGLSEC
     FVFFNDDVYL TAPVEPTDFF SDDGLPKYVT ALAPITTERY GTGHFQMNDM GIITTHFTRE
     EILKNGKFFS IKQGVKGIAK SLLYRHSKFI CGFWENHLTH PLLKSTMELV WEKEKDVLEK
     TSASRFRSPS DTNVWLFKYW QIASGQYAIG NPKLGGLFSL DNAGPDFWKL LNSRKYKVMC
     INDGFNVQNE NQVMDDFIKA MNQLFPDKSS FEI