ID   XCBA_NEIME              Reviewed;         486 AA.
AC   Q7X4S1;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Capsular polysaccharide phosphotransferase XcbA;
DE            EC=2.7.-.-;
DE   AltName: Full=Stealth protein XcbA;
GN   Name=xcbA;
OS   Neisseria meningitidis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=487;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN CAPSULE SYNTHESIS.
RC   STRAIN=M7575 / Serogroup X;
RX   PubMed=14638755; DOI=10.1128/iai.71.12.6712-6720.2003;
RA   Tzeng Y.-L., Noble C., Stephens D.S.;
RT   "Genetic basis for biosynthesis of the (alpha 1-->4)-linked N-acetyl-D-
RT   glucosamine 1-phosphate capsule of Neisseria meningitidis serogroup X.";
RL   Infect. Immun. 71:6712-6720(2003).
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 group II capsule biosynthesis locus.
CC   -!- FUNCTION: Part of a 3 gene operon, deletion of which prevents synthesis
CC       of the bacterial polysaccharide capsule. Capsule is important for the
CC       resistance of N.meningitidis serogroup X to killing by normal human
CC       serum. In Serogroup X the casule is a polymer of (alpha 1-->4)-linked
CC       N-acetylglucosamine 1-phosphate. This protein is probably the capsular
CC       polymerase.
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; AY289931; AAP44500.1; -; Genomic_DNA.
DR   RefSeq; WP_002234436.1; NZ_QQDX01000060.1.
DR   AlphaFoldDB; Q7X4S1; -.
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..486
FT                   /note="Capsular polysaccharide phosphotransferase XcbA"
FT                   /id="PRO_0000235957"
FT   REGION          38..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  56279 MW;  3782DC66633FE9C0 CRC64;
     MIMSKISKLV THPNLFFRDY FLKKAPLNYG ENIKPLPIET SSHSKKNTAH KTPVSSDQPI
     EDPYPVTFPI DVVYTWVDSD DEKFNEERLK FQNSSTSETL QGKAESTDIA RFQSRDELKY
     SIRSLMKYAP WVNHIYIVTN GQIPKWLDTN NTKVTIIPHS TIIDSQFLPT FNSHVIESSL
     YKIPGLSEHY IYFNDDVMLA RDLSPSYFFT SSGLAKLFIT NSRLPNGYKN VKDTPTQWAS
     KNSRELLHAE TGFWAEAMFA HTFHPQRKSV HESIEHLWHE QLNVCRQNRF RDISDINMAT
     FLHHHFAILT GQALATRTKC IYFNIRSPQA AQHYKTLLAR KGSEYSPHSI CLNDHTSSNK
     NILSNYEAKL QSFLETYYPD VSEAEILLPT KSEVAELVKH KDYLTVYTKL LPIINKQLVN
     KYNKPYSYLF YYLGLSARFL FEETQQEHYR ETAEENLQIF CGLNPKHTLA LKYLADVTLT
     SQPSGQ