GGTD_SYNY3
ID GGTD_SYNY3 Reviewed; 298 AA.
AC Q55473;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Osmoprotective compounds uptake permease protein GgtD {ECO:0000305};
GN Name=ggtD {ECO:0000303|PubMed:11081796};
GN OrderedLocusNames=slr0531 {ECO:0000312|EMBL:BAA10819.1};
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 (PubMed:11081796). Responsible for the translocation of
CC the substrate across the membrane (Probable).
CC {ECO:0000269|PubMed:11081796, ECO:0000305}.
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:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
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 binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
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DR EMBL; BA000022; BAA10819.1; -; Genomic_DNA.
DR PIR; S75972; S75972.
DR AlphaFoldDB; Q55473; -.
DR SMR; Q55473; -.
DR STRING; 1148.1001332; -.
DR TCDB; 3.A.1.1.32; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q55473; -.
DR EnsemblBacteria; BAA10819; BAA10819; BAA10819.
DR KEGG; syn:slr0531; -.
DR eggNOG; COG0395; Bacteria.
DR InParanoid; Q55473; -.
DR OMA; FNSMAAY; -.
DR PhylomeDB; Q55473; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..298
FT /note="Osmoprotective compounds uptake permease protein
FT GgtD"
FT /id="PRO_0000449364"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 91..283
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 298 AA; 32829 MW; 207EB2AB0945181A CRC64;
MTKAVNKSNR TNNTNRKTEF WQKLPIHIAI LTIAFIWTLP SLGLFISSLR PRGDMLSTGW
WTVFWHPLEI TQFYLGNYGD VLRSSGMGEA FLNSLTIAVP ATVIPIAIAT FAAYAFAWMT
FPGRQLLFIL VVCLLVVPLQ TTLIPVLRVY AQLGLAGTFL GVWLAHTAYG LPLGIYLLRN
YIGALPKDLI EAAAVDGASH LKIFTKLIVP LSMPAIASFA VFQFLWVWND LLVALVYLGG
TADVAPVTIQ LSNLVGSRGQ DWYLLTAGAF ISMIVPLMVF FGLQRYFVRG ILAGSVKS
