ID   SACB3_NEIMD             Reviewed;         545 AA.
AC   Q83U59;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 27.
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].
RC   STRAIN=M1124 / Serogroup A, M3562 / Serogroup A, and M7060 / Serogroup A;
RX   PubMed=14715772; DOI=10.1128/jcm.42.1.320-328.2004;
RA   Mothershed E.A., Sacchi C.T., Whitney A.M., Barnett G.A., Ajello G.W.,
RA   Schmink S., Mayer L.W., Phelan M., Taylor T.H. Jr., Bernhardt S.A.,
RA   Rosenstein N.E., Popovic T.;
RT   "Use of real-time PCR to resolve slide agglutination discrepancies in
RT   serogroup identification of Neisseria meningitidis.";
RL   J. Clin. Microbiol. 42:320-328(2004).
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: May be the polymerase that links individual UDP-N-acetyl-D-
CC       mannosamine monomers. In serotype A the capsule is composed of repeated
CC       units of (alpha 1-6)-linked N-acetyl-D-mannosamine-1-phosphate (By
CC       similarity). {ECO:0000250}.
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; AY234203; AAO85301.1; -; Genomic_DNA.
DR   EMBL; AY234205; AAO85303.1; -; Genomic_DNA.
DR   EMBL; AY281049; AAP34772.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q83U59; -.
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   3: Inferred from homology;
KW   Exopolysaccharide synthesis; Transferase.
FT   CHAIN           1..545
FT                   /note="Capsular polysaccharide phosphotransferase SacB"
FT                   /id="PRO_0000235952"
SQ   SEQUENCE   545 AA;  64134 MW;  7D2564286C95CD3D CRC64;
     MFILNNRKWR KLKRDPSAFF RDSKFNFLRY FSAKKFAKNF KNSSHIHKTN ISKAQSNISS
     TLKQNRKQDM LIPINFFNFE YIVKKLNNQN AIGVYILPSN LTLKPALCIL ESHKEDFLNK
     FLLTISSENL KLQYKFNGQI KNPKSVNEIW TDLFSIAHVD MKLSTDRTLS SSISQFWFRL
     EFCKEDKDFI LFPTANRYSR KLWKHSIKNN QLFKEGIRNY SEISSLPYEE DHNFDIDLVF
     TWVNSEDKNW QELYKKYKPD FNSDATSTSR FLSRDELKFA LRSWEMNGSF 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