ID   A0A3S8WYC9_9ACTN        Unreviewed;       738 AA.
AC   A0A3S8WYC9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Glycosyl transferase {ECO:0000313|EMBL:AZM61917.1};
GN   ORFNames=DLM49_22350 {ECO:0000313|EMBL:AZM61917.1};
OS   Streptomyces sp. WAC 01438.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2203204 {ECO:0000313|EMBL:AZM61917.1, ECO:0000313|Proteomes:UP000271045};
RN   [1] {ECO:0000313|EMBL:AZM61917.1, ECO:0000313|Proteomes:UP000271045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC 01438 {ECO:0000313|EMBL:AZM61917.1,
RC   ECO:0000313|Proteomes:UP000271045};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase
CC       family. {ECO:0000256|ARBA:ARBA00010488}.
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DR   EMBL; CP029601; AZM61917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S8WYC9; -.
DR   OrthoDB; 3183633at2; -.
DR   Proteomes; UP000271045; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047355; F:CDP-glycerol glycerophosphotransferase activity; IEA:InterPro.
DR   GO; GO:0019350; P:teichoic acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00761; Glyco_tranf_GTA_type; 1.
DR   Gene3D; 3.40.50.11820; -; 1.
DR   Gene3D; 3.40.50.12580; -; 1.
DR   InterPro; IPR007554; Glycerophosphate_synth.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR043148; TagF_C.
DR   InterPro; IPR043149; TagF_N.
DR   PANTHER; PTHR22916; GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR22916:SF76; GLYCOSYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF04464; Glyphos_transf; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271045};
KW   Teichoic acid biosynthesis {ECO:0000256|ARBA:ARBA00022944};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AZM61917.1}.
FT   DOMAIN          5..127
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   REGION          714..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   738 AA;  82595 MW;  B6725B2E49F256E7 CRC64;
     MPRFSIIVPV HKVQGYLHAC LDSVLGQSYR DIEVIAVDDR SPDGCGEILD GYAARDERVQ
     VLHLPENVGL GRARNAGMPH ATGDYLFFLD SDDTLTSGAL RALADRLDET GDPDVLIFDY
     ARTHWWGGTR RNALAHVLAD ASGGTFTAAE RPEILDLLMV VWNKVYRRDF VDREGFAFPP
     GYYEDTPWTF PVLLSAGRIA TLDRICLYYR QRRQGNILST TSRKHFDVHE QYARVFRFVD
     ARPALAHWRP FLHTKMGEHC LDILSKPDRL PPSDRGEFFR RTAEMFRLHR PEGVRVPAEL
     RVLEGGYAGY VLRRQAGQAG RELERRARQV RAGAAARAVR ARSVPRRPLD PRLAVYSAFS
     HRGVLGDPAA IYRAARELAP HIRGVWVLAD EEKAAGLPPD TEYVLLGSPG YRRATERATY
     LVNNVNWSGA LPKRPGSVHI HTHRGTPLKF MGADLLDRPG ARHGFDVPQM LRRADRWDYS
     LVANRHSELV WERAFPCHFT SLRSGSPRND VLVGAGPDSG RAVRARLGVP EGNTVVLYAP
     TRRDYRRDGL VERIDLARFA ADLGEGRTLV VRLHPSLADG PARGLGLTEL HRRGVLIDAT
     DEPEVQDVLL AADVLVTDYS ALMFDYALLD RPIVIHADDW DAFRASRGAY VDITAEAPGH
     VARSYRELVW LLESGTWQDE EAARLRSAFR QRYGEFDDGR AAERVVRALM LGEPLPEPAP
     GGDRVPAQAG SRDLLTPS
//