CPSY_MYCLE
ID CPSY_MYCLE Reviewed; 542 AA.
AC Q50025; O08112;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Exopolysaccharide phosphotransferase CpsY;
DE EC=2.7.-.-;
DE AltName: Full=Stealth protein CpsY;
GN Name=cpsY; OrderedLocusNames=ML2209; ORFNames=MLCB5.32c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; U15182; AAA62996.1; -; Genomic_DNA.
DR EMBL; Z95151; CAB08405.1; -; Genomic_DNA.
DR EMBL; AL583924; CAC31164.1; -; Genomic_DNA.
DR PIR; D87185; D87185.
DR RefSeq; NP_302449.1; NC_002677.1.
DR RefSeq; WP_010908769.1; NC_002677.1.
DR AlphaFoldDB; Q50025; -.
DR STRING; 272631.ML2209; -.
DR EnsemblBacteria; CAC31164; CAC31164; CAC31164.
DR KEGG; mle:ML2209; -.
DR PATRIC; fig|272631.5.peg.4184; -.
DR Leproma; ML2209; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_033996_0_0_11; -.
DR OMA; PTHNSQA; -.
DR Proteomes; UP000000806; 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; Reference proteome; Transferase.
FT CHAIN 1..542
FT /note="Exopolysaccharide phosphotransferase CpsY"
FT /id="PRO_0000235948"
FT REGION 522..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 61976 MW; C40CFE20223D54B2 CRC64;
MSKIVSCEDD RPVRRTLEPI IVTRQGKVAR LESSLTPHEA QIEDLIFLRK ALNRADIPFL
FIRNHKNRPV LAINIKLRPA VERALVTACA SEPMYAKTID ERGLSPVLVA KGQLSQSIDP
RIVRLYRRRI APGGFRFGSR FGVELQFWSF EETLIRCPVE NSLTRKVLPR KEVTPATIKL
YGYKWHTIEG MFTPHASDVT FDIDLVFSWV DGSDPEFRAR RAAEMSHHVV GEGDDADARI
RQIDELKYAL RSVNMFAPWI RRIFIATDSI PPSWLADHPM ITIVPAEDHF SDRSALPTYN
SHAVESQLHR IPDLSEHFLY SNDDMFFGRP LKASMFFSPG GVTRFIEAKT RIGLGTNDPT
RSGFENAARV NRQLLLRRFG QLITRHLEHT TVPLRKSVLF EMEQEFPEEF ARTQESVFRS
GTDISVTNSL YHYYALITGR AVQQEKAKVL YVDTTSYTGL NLLPELRKRR NYDFFCLNDG
SFPEVPATER AERVVSFLER YFPIPAPWEK VATDFNRQDF ASPTVSAPLE DGQTANPAQT
AR