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Database: UniProt
Entry: D9VZT7_9ACTN
LinkDB: D9VZT7_9ACTN
Original site: D9VZT7_9ACTN 
ID   D9VZT7_9ACTN            Unreviewed;       506 AA.
AC   D9VZT7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Undecaprenyl-phosphate glucose phosphotransferase {ECO:0000313|EMBL:EFL15697.1};
GN   ORFNames=SSNG_02949 {ECO:0000313|EMBL:EFL15697.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL15697.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL15697.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL15697.1,
RC   ECO:0000313|Proteomes:UP000005763};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain C.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC       {ECO:0000256|ARBA:ARBA00006464}.
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DR   EMBL; GG657750; EFL15697.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9VZT7; -.
DR   STRING; 253839.SSNG_02949; -.
DR   eggNOG; COG2148; Bacteria.
DR   HOGENOM; CLU_024920_0_1_11; -.
DR   Proteomes; UP000005763; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR003362; Bact_transf.
DR   InterPro; IPR017475; EPS_sugar_tfrase.
DR   NCBIfam; TIGR03025; EPS_sugtrans; 1.
DR   PANTHER; PTHR30576; COLANIC BIOSYNTHESIS UDP-GLUCOSE LIPID CARRIER TRANSFERASE; 1.
DR   PANTHER; PTHR30576:SF0; UNDECAPRENYL-PHOSPHATE N-ACETYLGALACTOSAMINYL 1-PHOSPHATE TRANSFERASE-RELATED; 1.
DR   Pfam; PF02397; Bac_transf; 1.
DR   Pfam; PF13727; CoA_binding_3; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFL15697.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        63..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          319..499
FT                   /note="Bacterial sugar transferase"
FT                   /evidence="ECO:0000259|Pfam:PF02397"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   506 AA;  53683 MW;  762AAE7EAB474B60 CRC64;
     MDSAPARHTG QGGTGHAGGS AFAPAAPAET RRAVTAIHPP RGPRADRARA AVRPQRARRR
     EGVTALLTAD ALAAAVTATT LPAGTLPPEA VLPAAALLTA LHAQAGLYRP RLAPSALREL
     PALAGRAAVL WAGAAALLAA AAPQRALGWS ALLGAIGLQV VLACAGRGSV NQLRRRAAVR
     RPVSALVVGP GEGTGAVAAA LHSRPEYGLR PVGIADTAAP ADGDPGQLPV LATHEDVRRA
     VIQNSVRHAV FTCPPEADER TASLVRLFHD HGCRLWLADP AGTAKITGMR VAQPADQLWG
     YAVQPLLPRP SRPLERAAKR AIDSCLAALA LLAAAPVMGV CALAVRLSDG PGVIFRQERV
     GLYGRPFTLL KFRTLRADEH ESATRWTVAG DRRMSPVGSF LRKSSLDELP QLWNVVRGDM
     SLVGPRPERP FFVAKFSTVH PGYEARHRMP VGITGLAQIN GLRGDTSIED RARFDNHYID
     TWSLWQDLWI LARTAASFFR FRLGGS
//
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