ID   CPS12_ACTPL             Reviewed;         371 AA.
AC   Q69AA9;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Capsular polysaccharide phosphotransferase cps12A;
DE            EC=2.7.-.-;
DE   AltName: Full=Stealth protein cps12A;
GN   Name=cps12A;
OS   Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=8329;
RA   Jessing S., Ahrens P., Angen Y.;
RT   "Cloning and sequencing of a serotype specific DNA region in Actinobacillus
RT   pleuropneumoniae serotype 12 and its application for PCR based
RT   identification.";
RL   Submitted (DEC-2003) 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).
RN   [3]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH NOD2 AND RIPK2, INTERACTION WITH
RP   RIPK1; RIPK2 AND RIPK3, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=21887730; DOI=10.1002/ibd.21851;
RA   Zhao Y., Alonso C., Ballester I., Song J.H., Chang S.Y., Guleng B.,
RA   Arihiro S., Murray P.J., Xavier R., Kobayashi K.S., Reinecker H.C.;
RT   "Control of NOD2 and Rip2-dependent innate immune activation by GEF-H1.";
RL   Inflamm. Bowel Dis. 18:603-612(2012).
CC   -!- FUNCTION: Part of a capsular polysaccharide synthesis locus.
CC       {ECO:0000269|PubMed:21887730}.
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; AY496881; AAS77490.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q69AA9; -.
DR   STRING; 228399.appser1_17000; -.
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   1: Evidence at protein level;
KW   Exopolysaccharide synthesis; Transferase.
FT   CHAIN           1..371
FT                   /note="Capsular polysaccharide phosphotransferase cps12A"
FT                   /id="PRO_0000235941"
SQ   SEQUENCE   371 AA;  43928 MW;  6CC842210CC7F46E CRC64;
     MNKMNRKFSK LLKNPHIFFR DFLNKKYPIK NTELPFSESE EANLIEANQK LDKIIQKNTL
     QQANIDVVFT WVDGSDPSWQ AKYSQYAPNY QAKSALYATD IARFEDHNEL YYSVHAVLKY
     MPWVRHIFII TDNQKPKWLD ETRQEKITLI DHQDIIDKEY LPTFNSHVIE AFLHKIPNLS
     ENFIYFNDDV FIARELQAEH FFQANGIASI FVSEKSLSKM RDKGIITPTL SASEYSIRLL
     NKYYDTNIDS PLVHTYIPLK KSMYELAWLR YEKAILGFLP NKLRTNNDLN FANFLIPWLM
     YFEGKAMPKI DICYYFNIRS PNAISLYKKL LLKQQMGEEP NSFCANDFNS NYSIENYRNN
     LISTLNNYYK F