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GGTA_SYNY3
ID   GGTA_SYNY3              Reviewed;         363 AA.
AC   Q79EE4; Q55035;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Osmoprotective compounds uptake ATP-binding protein GgtA {ECO:0000305};
DE            EC=7.5.2.- {ECO:0000305|PubMed:9006025};
GN   Name=ggtA {ECO:0000303|PubMed:9006025};
GN   OrderedLocusNames=slr0747 {ECO:0000312|EMBL:BAA18741.1};
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 [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   [2]
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   [3]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9006025; DOI=10.1128/jb.179.3.714-720.1997;
RA   Hagemann M., Richter S., Mikkat S.;
RT   "The ggtA gene encodes a subunit of the transport system for the
RT   osmoprotective compound glucosylglycerol in Synechocystis sp. strain PCC
RT   6803.";
RL   J. Bacteriol. 179:714-720(1997).
RN   [4]
RP   FUNCTION, AND SUBUNIT.
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:9006025, PubMed:11081796). Responsible for energy
CC       coupling to the transport system (Probable).
CC       {ECO:0000269|PubMed:11081796, ECO:0000269|PubMed:9006025, 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}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Transcription increases in cells adapted to higher salt
CC       concentrations, whereas transcription is weak in basal medium.
CC       {ECO:0000269|PubMed:9006025}.
CC   -!- DISRUPTION PHENOTYPE: Insertion mutant loses its GG uptake ability, and
CC       shows leakage of glucosylglycerol from the cells into the medium.
CC       Mutation does not affect salt tolerance. {ECO:0000269|PubMed:9006025}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; U32936; AAB41280.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18741.1; -; Genomic_DNA.
DR   PIR; S76829; S76829.
DR   AlphaFoldDB; Q79EE4; -.
DR   SMR; Q79EE4; -.
DR   IntAct; Q79EE4; 2.
DR   STRING; 1148.1653830; -.
DR   TCDB; 3.A.1.1.32; the atp-binding cassette (abc) superfamily.
DR   PaxDb; Q79EE4; -.
DR   EnsemblBacteria; BAA18741; BAA18741; BAA18741.
DR   KEGG; syn:slr0747; -.
DR   PATRIC; fig|1148.106.peg.3381; -.
DR   eggNOG; COG3842; Bacteria.
DR   InParanoid; Q79EE4; -.
DR   OMA; PRNMYDK; -.
DR   OrthoDB; 1200451at2; -.
DR   PhylomeDB; Q79EE4; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   CDD; cd03301; ABC_MalK_N; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015855; ABC_transpr_MalK-like.
DR   InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR040582; OB_MalK.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF17912; OB_MalK; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; SSF50331; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Sugar transport; Translocase; Transport.
FT   CHAIN           1..363
FT                   /note="Osmoprotective compounds uptake ATP-binding protein
FT                   GgtA"
FT                   /id="PRO_0000449361"
FT   DOMAIN          4..234
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   363 AA;  40756 MW;  8F97AED0BFD0FD94 CRC64;
     MASVSFEQVT KQFDDYVAVN NLNLEIEDGE FLVFVGPSGC GKTTSLRLLA GLETVSQGQI
     CIGDRRVNEL SPKDRDIAMV FQSYALYPHM SVYENMAFSL DLQGKPKEEI RQRVCSAAEL
     LGIEKLLHRK PKELSGGQRQ RVAVGRAIVR KPSVFLMDEP LSNLDAMLRV QARKEISKLH
     SDLATTFIYV THDQVEAMTM GDRIAVMKDG ILQQVDSPAN LYNQPANLFV AGFIGSPAMN
     FFQVERLSQE GKEKLSLDGV VLPMPDSVAK NGDRPLTLGI RPENIYHPQY LPLEIEPMEL
     PATVNLVEMM GNELIVYAQT PAGTEFVARI DPRVNIKQKD SVKFVVDTQR FYYFDREMET
     AIF
 
 
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