ID   STPA_SYNY3              Reviewed;         422 AA.
AC   Q55034; Q54787;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Glucosylglycerol-phosphate phosphatase;
DE            Short=GGP-P;
DE            EC=3.1.3.69 {ECO:0000269|PubMed:9045835};
DE   AltName: Full=Glucosylglycerol 3-phosphatase;
DE   AltName: Full=Salt tolerance protein A;
GN   Name=stpA; OrderedLocusNames=slr0746;
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 [GENOMIC DNA].
RA   Onana B., Jeanjean R., Joset F.;
RT   "A gene stpA involved in the establishment of salt tolerance in the
RT   cyanobacterium Synechocystis PCC6803.";
RL   Russ. J. Plant Physiol. 41:176-183(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8772170; DOI=10.1007/s002030050360;
RA   Hagemann M., Richter S., Zuther E., Schoor A.;
RT   "Characterization of a glucosylglycerol-phosphate-accumulating, salt-
RT   sensitive mutant of the cyanobacterium Synechocystis sp. strain PCC 6803.";
RL   Arch. Microbiol. 166:83-91(1996).
RN   [3]
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   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX   PubMed=9045835; DOI=10.1128/jb.179.5.1727-1733.1997;
RA   Hagemann M., Schoor A., Jeanjean R., Zuther E., Joset F.;
RT   "The stpA gene form synechocystis sp. strain PCC 6803 encodes the
RT   glucosylglycerol-phosphate phosphatase involved in cyanobacterial osmotic
RT   response to salt shock.";
RL   J. Bacteriol. 179:1727-1733(1997).
RN   [5]
RP   POSSIBLE INTERACTION WITH GGPS.
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: Phosphorylates glucosylglycerol-phosphate the precursor of
CC       the osmoprotectant glucosylglycerol necessary for salt adaptation of
CC       Synechocystis. {ECO:0000269|PubMed:9045835}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-O-(alpha-D-glucopyranosyl)-sn-glycerol 3-phosphate + H2O =
CC         2-O-(alpha-D-glucopyranosyl)glycerol + phosphate;
CC         Xref=Rhea:RHEA:22652, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:82766, ChEBI:CHEBI:87089; EC=3.1.3.69;
CC         Evidence={ECO:0000269|PubMed:9045835};
CC   -!- SUBUNIT: Monomer. Interacts with GGPS. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; U32936; AAB41279.1; -; Genomic_DNA.
DR   EMBL; X75566; CAA53245.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18740.1; -; Genomic_DNA.
DR   PIR; S76828; S76828.
DR   AlphaFoldDB; Q55034; -.
DR   IntAct; Q55034; 1.
DR   STRING; 1148.1653829; -.
DR   PaxDb; Q55034; -.
DR   EnsemblBacteria; BAA18740; BAA18740; BAA18740.
DR   KEGG; syn:slr0746; -.
DR   eggNOG; ENOG502Z8T5; Bacteria.
DR   OMA; VLTCGEH; -.
DR   BioCyc; MetaCyc:MON-20258; -.
DR   BRENDA; 3.1.3.69; 6192.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0050530; F:glucosylglycerol 3-phosphatase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR012765; GGPPase.
DR   Pfam; PF09506; Salt_tol_Pase; 1.
DR   PIRSF; PIRSF020945; GGPPase; 1.
DR   TIGRFAMs; TIGR02399; salt_tol_Pase; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..422
FT                   /note="Glucosylglycerol-phosphate phosphatase"
FT                   /id="PRO_0000114472"
FT   ACT_SITE        403
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        384
FT                   /note="D -> E (in Ref. 1; CAA53245)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  46542 MW;  E9C58CBC91A938F2 CRC64;
     MVLHQQRFSL DHGAFCQTLA QTENLLIVQD LDGVCMELVQ DPLSRRLDAD YVRATTLFAE
     HFYVLTNGEH VGKRGVQGIV EQSFGDASFV QQEGLYLPGL AAGGVQWQDR HGKVSHPGVG
     QTELEFLAAV PEKITNCLKT FFGDRPHSLS PEQLQTGIEA SVLDNVASPT ANLNTLANLL
     QDFPQIYRDL QETMAQLLDQ LMAEAVAQGL GNSFFVHYAP NLGRDERGKE IIRWAKAGDS
     GTTDFQFMLR GGVKEAGVLA LLNRYYHNRT GQYPLGESFS ARQAPPSHQD LLHLVKAQFD
     PALMPLIIGV GDTVTSQVDE ATGEIRRGGS DRQFLQLIQD LGDWGNHGNL VVYVDSSQGE
     VKNRQPLQLE TVAGQTQVVA GPGDMRDREE PLKINVAFPG GHDQYVAAFK QAAQRRRVHF
     SQ