ID   GGPS_SYNY3              Reviewed;         499 AA.
AC   P74258;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Glucosylglycerol-phosphate synthase;
DE            EC=2.4.1.213 {ECO:0000269|PubMed:9733686};
DE   AltName: Full=Glucosyl-glycerol-phosphate synthase;
DE            Short=GG-phosphate synthase;
DE            Short=GGPS;
GN   Name=ggpS; OrderedLocusNames=sll1566;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX   PubMed=9733686; DOI=10.1128/jb.180.18.4843-4849.1998;
RA   Marin K., Zuther E., Kerstan T., Kunert A., Hagemann M.;
RT   "The ggpS gene from Synechocystis sp. strain PCC 6803 encoding glucosyl-
RT   glycerol-phosphate synthase is involved in osmolyte synthesis.";
RL   J. Bacteriol. 180:4843-4849(1998).
RN   [3]
RP   SUBCELLULAR LOCATION, DEGRADATION BY FTSH2, AND POSSIBLE INTERACTION WITH
RP   GGP-P.
RX   PubMed=17116240; DOI=10.1111/j.1365-2958.2006.05495.x;
RA   Stirnberg M., Fulda S., Huckauf J., Hagemann M., Kramer R., Marin K.;
RT   "A membrane-bound FtsH protease is involved in osmoregulation in
RT   Synechocystis sp. PCC 6803: the compatible solute synthesizing enzyme GgpS
RT   is one of the targets for proteolysis.";
RL   Mol. Microbiol. 63:86-102(2007).
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:0000269|PubMed:9733686}.
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:0000269|PubMed:9733686};
CC   -!- PATHWAY: Glycan metabolism; glucosylglycerol biosynthesis.
CC   -!- SUBUNIT: Interacts with GGP-P. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17116240}.
CC   -!- PTM: Seems to be degraded, at least in vitro, by FtsH2. In an ftsH2
CC       disruption strain inactive GGPS accumulates.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC       {ECO:0000305}.
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DR   EMBL; BA000022; BAA18352.1; -; Genomic_DNA.
DR   PIR; S75893; S75893.
DR   AlphaFoldDB; P74258; -.
DR   SMR; P74258; -.
DR   IntAct; P74258; 1.
DR   STRING; 1148.1653438; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   PaxDb; P74258; -.
DR   EnsemblBacteria; BAA18352; BAA18352; BAA18352.
DR   KEGG; syn:sll1566; -.
DR   eggNOG; COG0380; Bacteria.
DR   InParanoid; P74258; -.
DR   OMA; YYGFSNR; -.
DR   PhylomeDB; P74258; -.
DR   BioCyc; MetaCyc:MON-20259; -.
DR   BRENDA; 2.4.1.213; 6192.
DR   UniPathway; UPA00795; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Cytoplasm; Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..499
FT                   /note="Glucosylglycerol-phosphate synthase"
FT                   /id="PRO_0000122506"
SQ   SEQUENCE   499 AA;  56802 MW;  7D4C279DB5EBAF8F CRC64;
     MNSSLVILYH REPYDEVREN GKTVYREKKS PNGILPTLKS FFADAEQSTW VAWKQVSPKQ
     KDDFQADMSI EGLGDRCTVR RVPLTAEQVK NFYHITSKEA FWPILHSFPW QFTYDSSDWD
     NFQHINRLFA EAACADADDN ALFWVHDYNL WLAPLYIRQL KPNAKIAFFH HTPFPSVDIF
     NILPWREAIV ESLLACDLCG FHIPRYVENF VAVARSLKPV EITRRVVVDQ AFTPYGTALA
     EPELTTQLRY GDRLINLDAF PVGTNPANIR AIVAKESVQQ KVAEIKQDLG GKRLIVSAGR
     VDYVKGTKEM LMCYERLLER RPELQGEISL VVPVAKAAEG MRIYRNAQNE IERLAGKING
     RFAKLSWTPV MLFTSPLAYE ELIALFCAAD IAWITPLRDG LNLVAKEYVV AKNGEEGVLI
     LSEFAGCAVE LPDAVLTNPY ASSRMDESID QALAMDKDEQ KKRMGRMYAA IKRYDVQQWA
     NHLLREAYAD VVLGEPPQM