ID   LCBA_NEIME              Reviewed;         366 AA.
AC   Q9RGR0;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Capsular polysaccharide phosphotransferase LcbA;
DE            EC=2.7.-.-;
DE   AltName: Full=Stealth protein LcbA;
GN   Name=lcbA;
OS   Neisseria meningitidis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=487;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serogroup L;
RA   Brewer N.E., Coulthart M.B., Tyler S.D.;
RT   "Analysis of the region encoding the putative capsular biosynthetic genes
RT   of the Neisseria meningitidis serogroup L.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; AF112478; AAF21950.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RGR0; -.
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   Pfam; PF17101; Stealth_CR1; 1.
DR   Pfam; PF11380; Stealth_CR2; 1.
PE   3: Inferred from homology;
KW   Exopolysaccharide synthesis; Transferase.
FT   CHAIN           1..366
FT                   /note="Capsular polysaccharide phosphotransferase LcbA"
FT                   /id="PRO_0000235956"
SQ   SEQUENCE   366 AA;  43281 MW;  F7A95F3843D1B67E CRC64;
     MKRLKKLTRE PGVFFRDYFN KKYPVRNIEQ RINEIEEPAI IANSLHLAAV ESAIHLSPFK
     IDVVFTWVDN SDTQWQQRHQ QYCHAASPNN LYSNDETRFA NHNELYYSLH SVRSFLPWVN
     HIYIITDSQT PKWFKSAEYP NVSIIDHSEI IDKQYLPTFN SHVIEAHLHN IPNLSEHFIY
     FNDDVFVARP LHREHFFHAN GIASLFIADK SLQKMATKGT ITPTLSASQN CIRLLNQRYD
     CNLDHPLVHT YVPLRKSGFQ TAWQYYREEI KAFLPNKFRT NQDLNLATFL VPWLMYLDGK
     SIPNNDICYY FNIRSNKAPT QYLKLLQKNE DNQQPHSFCA NDFHSEQQLY DYHAKLIAML
     KDYFKI