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GLPF_BACSU
ID   GLPF_BACSU              Reviewed;         274 AA.
AC   P18156;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Glycerol uptake facilitator protein {ECO:0000250|UniProtKB:P0AER0};
GN   Name=glpF; OrderedLocusNames=BSU09280;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8436953; DOI=10.1099/00221287-139-2-349;
RA   Beijer L., Nilsson R.-P., Holmberg C., Rutberg L.;
RT   "The glpP and glpF genes of the glycerol regulon in Bacillus subtilis.";
RL   J. Gen. Microbiol. 139:349-359(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA   Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA   Venema G., Bron S.;
RT   "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT   subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT   many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL   Microbiology 144:859-875(1998).
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-274.
RX   PubMed=2127799; DOI=10.1099/00221287-136-12-2367;
RA   Holmberg C., Beijer L., Rutberg B., Rutberg L.;
RT   "Glycerol catabolism in Bacillus subtilis: nucleotide sequence of the genes
RT   encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase
RT   (glpD).";
RL   J. Gen. Microbiol. 136:2367-2375(1990).
CC   -!- FUNCTION: Mediates glycerol diffusion across the cytoplasmic membrane
CC       via a pore-type mechanism. {ECO:0000250|UniProtKB:P0AER0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycerol(in) = glycerol(out); Xref=Rhea:RHEA:29675,
CC         ChEBI:CHEBI:17754; Evidence={ECO:0000250|UniProtKB:P0AER0};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Requires glycerol 3-phosphate and the GlpP product;
CC       repressed by glucose.
CC   -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC       membrane-spanning domains and a pore-forming loop with the signature
CC       motif Asn-Pro-Ala (NPA). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC       {ECO:0000305}.
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DR   EMBL; M99611; AAA22490.1; -; Genomic_DNA.
DR   EMBL; Y14079; CAA74428.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12756.1; -; Genomic_DNA.
DR   EMBL; M34393; AAA22485.1; ALT_SEQ; Genomic_DNA.
DR   PIR; C47700; C47700.
DR   RefSeq; NP_388809.1; NC_000964.3.
DR   RefSeq; WP_003233386.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P18156; -.
DR   SMR; P18156; -.
DR   STRING; 224308.BSU09280; -.
DR   TCDB; 1.A.8.2.1; the major intrinsic protein (mip) family.
DR   PaxDb; P18156; -.
DR   PRIDE; P18156; -.
DR   EnsemblBacteria; CAB12756; CAB12756; BSU_09280.
DR   GeneID; 939266; -.
DR   KEGG; bsu:BSU09280; -.
DR   PATRIC; fig|224308.179.peg.1001; -.
DR   eggNOG; COG0580; Bacteria.
DR   InParanoid; P18156; -.
DR   OMA; MTRTGMF; -.
DR   PhylomeDB; P18156; -.
DR   BioCyc; BSUB:BSU09280-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:0015254; F:glycerol channel activity; IBA:GO_Central.
DR   GO; GO:0015793; P:glycerol transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
DR   TIGRFAMs; TIGR00861; MIP; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..274
FT                   /note="Glycerol uptake facilitator protein"
FT                   /id="PRO_0000064077"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           64..66
FT                   /note="NPA 1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           185..187
FT                   /note="NPA 2"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   274 AA;  28735 MW;  8624D0046A63075D CRC64;
     MTAFWGEVIG TMLLIIFGAG VCAGVNLKKS LSFQSGWIVV VFGWGLGVAM AAYAVGGISG
     AHLNPALTIA LAFVGDFPWK EVPVYIAAQM IGAIIGAVII YLHYLPHWKS TDDPAAKLGV
     FSTGPSIPHT FANVLSEVIG TFVLVLGILA IGANQFTEGL NPLIVGFLIV AIGISLGGTT
     GYAINPARDL GPRIAHAFLP IPGKGSSNWK YAWVPVVGPI LGGSFGGVFY NAAFKGHITS
     SFWIVSVILV VVLLGLYVYT KSHSAKTLSN SKYI
 
 
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