ID   GGPS_SYNP2              Reviewed;         500 AA.
AC   O65979; B1XNA9;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Glucosylglycerol-phosphate synthase;
DE            EC=2.4.1.213;
DE   AltName: Full=Glucosyl-glycerol-phosphate synthase;
DE            Short=GG-phosphate synthase;
DE            Short=GGPS;
GN   Name=ggpS; OrderedLocusNames=SYNPCC7002_A2851;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10543792; DOI=10.1128/aem.65.11.4822-4829.1999;
RA   Engelbrecht F., Marin K., Hagemann M.;
RT   "Expression of the ggpS gene, involved in osmolyte synthesis in the marine
RT   cyanobacterium synechococcus sp. strain PCC 7002, revealed regulatory
RT   differences between this strain and the freshwater strain synechocystis sp.
RT   strain PCC 6803.";
RL   Appl. Environ. Microbiol. 65:4822-4829(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in salt tolerance by producing GG-phosphate from
CC       ADP-glucose and glycerol-3-phosphate (G3P), an intermediate in the
CC       synthesis of the osmolyte glucosylglycerol (GG).
CC       {ECO:0000250|UniProtKB:P74258}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-alpha-D-glucose + sn-glycerol 3-phosphate = 2-O-(alpha-D-
CC         glucopyranosyl)-sn-glycerol 3-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:12881, ChEBI:CHEBI:15378, ChEBI:CHEBI:57498,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:87089, ChEBI:CHEBI:456216;
CC         EC=2.4.1.213; Evidence={ECO:0000250|UniProtKB:P74258};
CC   -!- PATHWAY: Glycan metabolism; glucosylglycerol biosynthesis.
CC   -!- INDUCTION: By salt shock.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ006298; CAA06963.1; -; Genomic_DNA.
DR   EMBL; CP000951; ACB00819.1; -; Genomic_DNA.
DR   RefSeq; WP_012308437.1; NC_010475.1.
DR   AlphaFoldDB; O65979; -.
DR   SMR; O65979; -.
DR   STRING; 32049.SYNPCC7002_A2851; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   EnsemblBacteria; ACB00819; ACB00819; SYNPCC7002_A2851.
DR   KEGG; syp:SYNPCC7002_A2851; -.
DR   eggNOG; COG0380; Bacteria.
DR   HOGENOM; CLU_002351_7_1_3; -.
DR   OMA; YYGFSNR; -.
DR   UniPathway; UPA00795; -.
DR   Proteomes; UP000001688; Chromosome.
DR   GO; GO:0033828; F:glucosylglycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051473; P:glucosylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   CDD; cd03788; GT20_TPS; 1.
DR   InterPro; IPR012764; Gluc_glyc_Psyn.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   PANTHER; PTHR10788; PTHR10788; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   TIGRFAMs; TIGR02398; gluc_glyc_Psyn; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Reference proteome; Stress response; Transferase.
FT   CHAIN           1..500
FT                   /note="Glucosylglycerol-phosphate synthase"
FT                   /id="PRO_0000122505"
FT   CONFLICT        364
FT                   /note="K -> N (in Ref. 1; CAA06963)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  57169 MW;  94543DCFE6AD8819 CRC64;
     MKSSLVILYH REPYDEVREN GKTFYRDKTS PNGIMPTLKS FFANAEQSTW VAWKQISGKQ
     QENFQAKMAF PGQENSVVHR IPLSADQVKN FYHITSKEAF WPILHSFPWQ FTYDSSDWEN
     FKQINEMFAE AACEDADDDA LFWVHDYNLW LTPYFIRQKK PNAKIAFFHH TPFPSVDIFN
     ILPWREAIVD SLLCCDLCGF HLPRYVQNFV AVARSLRKVE ITRQVPVDEH AFTAVGTALA
     EPEITTQLKY KDHLVNLDAF PVGTNPTQIR AQVEKASTQE RIRKIREELG SNKLILSAGR
     VDYVKGTKEM LVCYERLLER RPELQTKVNL VVAAAKAASG MRVYKNAQSE IERLVGRING
     RFAKLNWTPI LLFTSALSYE ELLGFFGAAD IAWITPLRDG LNLVAKEYVV AHGCDDGVLI
     LSEFAGSAVE LPDAILTNPY AAKRMDESID QALAMPVEEQ QRRMKSMYQA IQRYDVQQWA
     NHMFREAKAT AVLGKEPTPV