ID   Y6022_STRCO             Reviewed;         540 AA.
AC   O69852;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Exopolysaccharide phosphotransferase SCO6022;
DE            EC=2.7.-.-;
DE   AltName: Full=Stealth protein SCO6022;
GN   OrderedLocusNames=SCO6022; ORFNames=SC1C3.10;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939126; CAA19234.1; -; Genomic_DNA.
DR   PIR; T34702; T34702.
DR   RefSeq; NP_630133.1; NC_003888.3.
DR   RefSeq; WP_003972901.1; NZ_VNID01000009.1.
DR   AlphaFoldDB; O69852; -.
DR   STRING; 100226.SCO6022; -.
DR   GeneID; 1101463; -.
DR   KEGG; sco:SCO6022; -.
DR   PATRIC; fig|100226.15.peg.6122; -.
DR   eggNOG; COG0438; Bacteria.
DR   HOGENOM; CLU_033996_0_0_11; -.
DR   OMA; HYGRARV; -.
DR   PhylomeDB; O69852; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Exopolysaccharide synthesis; Reference proteome; Transferase.
FT   CHAIN           1..540
FT                   /note="Exopolysaccharide phosphotransferase SCO6022"
FT                   /id="PRO_0000235962"
SQ   SEQUENCE   540 AA;  59489 MW;  9282D034DBD98A86 CRC64;
     MANPTSMSSA VHVYRRFVPQ PVRSAAATTV PAGVRRKVKG GLARTLSRRE ARLHRRALRR
     VRRAGLGQSE RRTTAPDGRI AHVHTGLTVD LARRLDHDLV THALDAAEVP WFAVPALDDR
     RLCLAVEVRD KGTVRRVLRA LLEEHTGYVV SVSPSAADTR ETPGSHIKAW KHYGRARVIR
     LTWLRTDPTE GLWVGEDQGI EIEFWTANTD LPHERLIGPR PNRVQRAVPA EALGIEIGLD
     RLSGYCDIDG DLGPTVTLEN FDVVRLEEIS FPVDAVLLWQ HPTPWGEELL RAALRSVHQY
     APWIDVVHVV AQAEPPAWLE ADERISVVRA VPGAEWRLDQ LPDLAEHFLL MRPGALLGRP
     VRPFDYFTPG GGTRPRRGPW NASESFAEWV RAAYSVTGRA TGHGYAAGPQ PYRADTLTRL
     GEAGARSLPV PDEQVLSGVP GTHPMDGMAH HFGYVAGHAD PSGEASVALH AALPGIGTHL
     QRLLVRRDVQ QLQFFGLGTG EAGSGGGTNA VVRFLHQYYP VPSVFECDRP QTDTEPDRHS