ID   GGTB_SYNY3              Reviewed;         421 AA.
AC   Q55471;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Osmoprotective compounds-binding protein GgtB {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ggtB {ECO:0000303|PubMed:11081796};
GN   OrderedLocusNames=slr0529 {ECO:0000312|EMBL:BAA10817.1};
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, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11081796; DOI=10.1007/s002030000201;
RA   Mikkat S., Hagemann M.;
RT   "Molecular analysis of the ggtBCD gene cluster of Synechocystis sp. strain
RT   PCC6803 encoding subunits of an ABC transporter for osmoprotective
RT   compounds.";
RL   Arch. Microbiol. 174:273-282(2000).
CC   -!- FUNCTION: Part of the ABC transporter complex GgtABCD involved in the
CC       uptake of the osmoprotective compounds glucosylglycerol (GG), sucrose
CC       and trehalose. Binds glucosylglycerol and exhibits a somewhat lower
CC       affinity towards sucrose and a substantially lower affinity towards
CC       trehalose. {ECO:0000269|PubMed:11081796}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GgtA),
CC       two transmembrane proteins (GgtC and GgtD) and a solute-binding protein
CC       (GgtB). {ECO:0000305|PubMed:11081796}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- INDUCTION: Expression is very low in cells grown in basal medium but
CC       increases significantly after a salt shock.
CC       {ECO:0000269|PubMed:11081796}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation of the gene results in loss of the
CC       ability to take up glucosylglycerol and sucrose, as well as to
CC       accumulate exogenous trehalose. Insertion causes leakage of
CC       glucosylglycerol from the cells into the medium.
CC       {ECO:0000269|PubMed:11081796}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC       {ECO:0000305}.
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DR   EMBL; BA000022; BAA10817.1; -; Genomic_DNA.
DR   PIR; S75970; S75970.
DR   AlphaFoldDB; Q55471; -.
DR   SMR; Q55471; -.
DR   IntAct; Q55471; 1.
DR   STRING; 1148.1001330; -.
DR   TCDB; 3.A.1.1.32; the atp-binding cassette (abc) superfamily.
DR   PaxDb; Q55471; -.
DR   EnsemblBacteria; BAA10817; BAA10817; BAA10817.
DR   KEGG; syn:slr0529; -.
DR   eggNOG; COG1653; Bacteria.
DR   InParanoid; Q55471; -.
DR   OMA; KPWCAGI; -.
DR   PhylomeDB; Q55471; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   InterPro; IPR006059; SBP.
DR   Pfam; PF01547; SBP_bac_1; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW   Signal; Sugar transport; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           19..421
FT                   /note="Osmoprotective compounds-binding protein GgtB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_0000449362"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   421 AA;  46473 MW;  0ED023CDB7DA8F34 CRC64;
     MKFFKITTLI ISLIVLTSCQ GPGVNGDEDR KQVTILGVMI GEQQEKIEQA LAPFTEATGI
     EVVYEGVDTF ATTLPIRVDS GRAPDLAMFP QPGLMADFAR EGKLVPLGEI LTPEEMTEAY
     DQAWLDLAAV DGTVYGVWYR ASVKSLVWFN PQEFAANGYE VPGTWEEMMA LSQRLIDKGK
     TPWCLGIESG NATGWVGTDW VEDIMLRTAS PATYDQWVAH DIPFNDRRVE NALDIFGEIT
     QNEKMIYGGK VGALSTPFGD SILGLFTDPP HCYLHRQGNF IAAFLPADVD DDQVDIFPLP
     PIEEEYGLPI LVAGDIFAMF NDTPEARQLM AYLASSRPHE VAATLGAYIS PHKNIDLNLY
     PDRLTRKQAE ILNKAEVIRF DASDMMPGAV GTGTFWSGMV DYIGGADGTQ VLNTIERSWP
     R