GLPT_BACSU
ID GLPT_BACSU Reviewed; 444 AA.
AC P37948;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glycerol-3-phosphate transporter;
DE Short=G-3-P transporter;
DE AltName: Full=G-3-P permease;
GN Name=glpT; Synonyms=ybeE; OrderedLocusNames=BSU02140;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BR95;
RX PubMed=8012593; DOI=10.1099/00221287-140-4-723;
RA Nilsson R.P., Beijer L., Rutberg B.;
RT "The glpT and glpQ genes of the glycerol regulon in Bacillus subtilis.";
RL Microbiology 140:723-730(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT Bacillus subtilis chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Responsible for glycerol-3-phosphate uptake.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family. {ECO:0000305}.
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DR EMBL; Z26522; CAA81291.1; -; Genomic_DNA.
DR EMBL; AB006424; BAA33111.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12008.1; -; Genomic_DNA.
DR PIR; I40417; I40417.
DR RefSeq; NP_388096.1; NC_000964.3.
DR RefSeq; WP_003246460.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P37948; -.
DR SMR; P37948; -.
DR STRING; 224308.BSU02140; -.
DR PaxDb; P37948; -.
DR PRIDE; P37948; -.
DR EnsemblBacteria; CAB12008; CAB12008; BSU_02140.
DR GeneID; 938447; -.
DR KEGG; bsu:BSU02140; -.
DR PATRIC; fig|224308.179.peg.220; -.
DR eggNOG; COG2271; Bacteria.
DR InParanoid; P37948; -.
DR OMA; AMPYLID; -.
DR PhylomeDB; P37948; -.
DR BioCyc; BSUB:BSU02140-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0061513; F:glucose 6-phosphate:inorganic phosphate antiporter activity; IBA:GO_Central.
DR GO; GO:0015169; F:glycerol-3-phosphate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015760; P:glucose-6-phosphate transport; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR005267; G3P_transporter.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR021159; Sugar-P_transporter_CS.
DR InterPro; IPR000849; Sugar_P_transporter.
DR Pfam; PF07690; MFS_1; 1.
DR PIRSF; PIRSF002808; Hexose_phosphate_transp; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00712; glpT; 1.
DR PROSITE; PS00942; GLPT; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycerol metabolism; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..444
FT /note="Glycerol-3-phosphate transporter"
FT /id="PRO_0000199877"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 37..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 58..63
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 64..84
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 85..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 94..112
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 113..120
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 121..141
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 142..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 161..180
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 181..189
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 190..207
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 208..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 262..282
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 283..287
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 288..308
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250"
FT TOPO_DOM 309..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 322..341
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250"
FT TOPO_DOM 342..346
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 347..368
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250"
FT TOPO_DOM 369..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 388..409
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250"
FT TOPO_DOM 410..414
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 415..435
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250"
FT TOPO_DOM 436..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 444 AA; 49802 MW; E776BAA5C71DB2BA CRC64;
MLNIFKPAPH IERLDDSKMD AAYKRLRLQV FIGIFIGYAG YYLLRKNFAF AIPYLQEQGF
SKTELGLVLA AVSIAYGFSK FIMGMVSDRC NPRYFLATGL FLSAIVNILF VSMPWVTSSV
TIMFIFMFIN GWFQGMGWPP CGRTMAHWFS ISERGTKMSI WNVAHNIGGG ILAPLVTLGI
AMFVTWKSVF FFPAIIAIII SFLIVLLVRD TPQSCGLPPI EEYRNDYPKH AFKNQEKELT
TKEILFQYVL NNKFLWYIAF ANVFVYFVRY GVVDWAPTYL TEAKGFSPED SRWSYFLYEY
AGIPGTILCG WISDRFFKSR RAPAGVLFMA GVFIAVLVYW LNPAGNPLVD NIALISIGFL
IYGPVMLIGL QAIDLAPKKA AGTAAGLTGF FGYIGGSAFA NAIMGFVVDR FNWNGGFIML
ISSCILAIVF LALTWNTGKR AEHV
