SACB_NEIMA
ID SACB_NEIMA Reviewed; 545 AA.
AC Q9JWW8; A1IP55;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Capsular polysaccharide phosphotransferase SacB;
DE EC=2.7.-.-;
DE AltName: Full=Stealth protein SacB;
GN Name=sacB; OrderedLocusNames=NMA0200;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
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; AL157959; CAM07514.1; -; Genomic_DNA.
DR PIR; C82014; C82014.
DR RefSeq; WP_002236578.1; NC_003116.1.
DR AlphaFoldDB; Q9JWW8; -.
DR EnsemblBacteria; CAM07514; CAM07514; NMA0200.
DR KEGG; nma:NMA0200; -.
DR HOGENOM; CLU_499510_0_0_4; -.
DR BioCyc; NMEN122587:NMA_RS01030-MON; -.
DR Proteomes; UP000000626; Chromosome.
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_0000235950"
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