ID   SACB2_NEIMD             Reviewed;         545 AA.
AC   O68215;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Capsular polysaccharide phosphotransferase SacB;
DE            EC=2.7.-.-;
DE   AltName: Full=Stealth protein SacB;
GN   Name=sacB;
OS   Neisseria meningitidis serogroup A.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=65699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND DISCUSSION OF
RP   FUNCTION.
RC   STRAIN=F8229 / Serogroup A;
RX   PubMed=9515923; DOI=10.1128/jb.180.6.1533-1539.1998;
RA   Swartley J.S., Liu L.-J., Miller Y.K., Martin L.E., Edupuganti S.,
RA   Stephens D.S.;
RT   "Characterization of the gene cassette required for biosynthesis of the
RT   (alpha1->6)-linked N-acetyl-D-mannosamine-1-phosphate capsule of serogroup
RT   A Neisseria meningitidis.";
RL   J. Bacteriol. 180:1533-1539(1998).
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 a capsular biosynthesis operon and has been suggested
CC       to be the polymerase that links individual UDP-N-acetyl-D-mannosamine
CC       monomers. In serotype A the capsule is composed of repeated units of
CC       (alpha 1-6)-linked N-acetyl-D-mannosamine-1-phosphate. Non-polar
CC       disruption of this open reading frame prevented capsule synthesis.
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; AF019760; AAC38286.1; -; Genomic_DNA.
DR   AlphaFoldDB; O68215; -.
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   InterPro; IPR031356; Stealth_CR4.
DR   Pfam; PF17101; Stealth_CR1; 1.
DR   Pfam; PF11380; Stealth_CR2; 1.
DR   Pfam; PF17102; Stealth_CR3; 1.
DR   Pfam; PF17103; Stealth_CR4; 1.
PE   1: Evidence at protein level;
KW   Exopolysaccharide synthesis; Transferase.
FT   CHAIN           1..545
FT                   /note="Capsular polysaccharide phosphotransferase SacB"
FT                   /id="PRO_0000235951"
SQ   SEQUENCE   545 AA;  64098 MW;  1BC3400C5CC33DCD CRC64;
     MFILNNRKWR KLKRDPSAFF RDSKFNFLRY FSAKKFAKNF KNSSHIHKTN ISKAQSNISS
     TLKENRKQDM LIPINFFNFE YIVKKLNNQN AIGVYILPSN LTLKPALCIL ESHKEDFLNK
     FLLTISSENL KLQYKFNGQI KNPKSVNEIW TDLFSIAHVD MKLSTDRTLS SSISQFWFRL
     EFCKEDKDFI LFSTANRYSR KLWKHSIKNN QLFKEGIRNY SEISSLPYEE DHNFDIDLVF
     TWVNSEDKNW QELYKKYKPD FNSDATSTSR FLSRDELKFA LRSWEMSGSF IRKIFIVSNC
     APPAWLDLNN PKIQWVYHEE IMPQSALPTF SSHAIETSLH HIPGISNYFI YSNDDFLLTK
     PLNKDNFFYS NGIAKLRLEA WGNVNGECTE GEPDYLNGAR NANTLLEKEF KKFTTKLHTH
     SPQSMRTDIL FEMEKKYPEE FNRTLHNKFR SLDDIAVTGY LYHHYALLSG RALQSSDKTE
     LVQQNHDFKK KLNNVVTLTK ERNFDKLPLS VCINDGADSH LNEEWNVQVI KFLETLFPLP
     SSFEK