ID   V6JZV1_9ACTN            Unreviewed;      1228 AA.
AC   V6JZV1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Glycosyltransferase 2-like domain-containing protein {ECO:0000259|Pfam:PF00535};
DE   Flags: Fragment;
GN   ORFNames=N566_26750 {ECO:0000313|EMBL:EST22194.1};
OS   Streptomycetaceae bacterium MP113-05.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae.
OX   NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST22194.1, ECO:0000313|Proteomes:UP000017915};
RN   [1] {ECO:0000313|EMBL:EST22194.1, ECO:0000313|Proteomes:UP000017915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP113-05 {ECO:0000313|EMBL:EST22194.1,
RC   ECO:0000313|Proteomes:UP000017915};
RA   Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT   "Streptomyces bacterium from a marine sponge: physiological
RT   characterization and genome-based analysis of secondary metabolite
RT   biosynthesis potential.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase
CC       family. {ECO:0000256|ARBA:ARBA00010488}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EST22194.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWQV01000868; EST22194.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6JZV1; -.
DR   STRING; 1380770.N566_26750; -.
DR   HOGENOM; CLU_003394_1_0_11; -.
DR   OrthoDB; 3183633at2; -.
DR   Proteomes; UP000017915; Unassembled WGS sequence.
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; PTHR37316; TEICHOIC ACID GLYCEROL-PHOSPHATE PRIMASE; 1.
DR   PANTHER; PTHR37316:SF3; TEICHOIC ACID GLYCEROL-PHOSPHATE TRANSFERASE; 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:UP000017915};
KW   Teichoic acid biosynthesis {ECO:0000256|ARBA:ARBA00022944};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..152
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   REGION          71..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..645
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1228
FT                   /evidence="ECO:0000313|EMBL:EST22194.1"
SQ   SEQUENCE   1228 AA;  135147 MW;  0416B2A894670BA1 CRC64;
     MSPRLSVVVP LHTTGARLLP CLRSLAAQTM ADLEVVLVDD ALDDTPDDAP EGSSVVAAAR
     EFASGDGRFR VVRDGSGPPE ASGDRGRARN AGLRHTDPQT PYVAFLDPED TLPATAYERL
     LGTLEASGSD FATGNAVRVG PDGRAGRTPL LGRPLDRDRP AVHVTRHRNL VRDRMTGNKV
     FRRTFWERQA LSWAENTGEP DLRLIVPAHF LATAVDVVGG PVLHRHEASG GGTETGPPAA
     GTPRARAAGR GAELRELVRA LDAVSRFVNG RHSSKRRRRG EPGRHFDTLA LSHDLAPYLA
     ALLDADAPFQ AEFASVASDF LSHLDPAVVV SLPLPARIKW YLVRAGRIED LLAALAFERD
     NPRVLHLTGS GTRRTASYLR PDGSRIEVPH RIGRVRSGEQ PMHARLTEAR RQPDGTLLLR
     GYGYIRSADA DRPQRSRKFG WLRQGDGSHR RLPLRVRTVP APEATRNSRQ RTYSYDASGF
     EITVDPQRLL TALRRGRRSA SWTVCLGVAT GALVRSGGVR AGSDGTGAQP PVCELPGDRR
     MSATFSNGRL RLLVEETVAR LSGQRATDGT WRPEFTVRRP HRPTALRMTH QPSGSELELP
     VPPEAAADGD DWAGYSVTVP LDALTASPDR GHEEEGEDGS DESRPGGSGR WRLSLLLADG
     STCRIVVPPG APPLSAPFPH SGEPGDGEAP RELYASPDAL GHLTLTARCV HPVAGRLTWT
     DRGELALEGE LPRSVPAGLE AVWQHSGHRQ EVTVPLERHG DRFATRLSPA DAAPGGLPLR
     QGRWFPFLRP VGAGTREHDL PVRLDPGLLD TLPQRCEGSG AGARTFTAER RYGERLFLHS
     GSDLEPTERG AYGQHRLSTL HYPEARRLPL RDAVLYHSFD GRQYSDSPRA VHEELVRRGT
     DVEHLWVVRD GQALVPPSAE PVVMGSARWY EALARSRWLI GNTHFPRCFA RRDGQTAVQT
     WHGTPLKRIG HDLADTDFAN RSYLAGLTAR AAEWSVLLSP NRFSTPILRR AFGYTGEVLE
     SGYPRNDRLY AEDRERRAEH VRRRLGIPAG TRVVLYAPTW RDDDRYDRTN CRFDLRLDLA
     AAHAALGDDH VLLVRKHYLV ADTVPSTADG FVRDVSAHSD LAELLLIADV LITDYSSVMF
     DFAHTGRPML FHTYDLDHYR DVLRGFYFDF EKRAPGPLLS SSDEVITALR EVDAVADAHQ
     EAYADFRRSF CDLDDGTAAA RVADRMFG
//