GLPP_BACSU
ID GLPP_BACSU Reviewed; 192 AA.
AC P30300;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glycerol uptake operon antiterminator regulatory protein;
GN Name=glpP; Synonyms=glpP1; OrderedLocusNames=BSU09270;
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=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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=4368746; DOI=10.1128/jb.119.2.431-442.1974;
RA Lindgren V., Rutberg L.;
RT "Glycerol metabolism in Bacillus subtilis: gene-enzyme relationships.";
RL J. Bacteriol. 119:431-442(1974).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=182672; DOI=10.1128/jb.127.3.1047-1057.1976;
RA Lindgren V., Rutberg L.;
RT "Genetic control of the glp system in Bacillus subtilis.";
RL J. Bacteriol. 127:1047-1057(1976).
RN [6]
RP FUNCTION.
RC STRAIN=168 / BR95;
RX PubMed=1809833; DOI=10.1111/j.1365-2958.1991.tb01849.x;
RA Holmberg C., Rutberg B.;
RT "Expression of the gene encoding glycerol-3-phosphate dehydrogenase (glpD)
RT in Bacillus subtilis is controlled by antitermination.";
RL Mol. Microbiol. 5:2891-2900(1991).
RN [7]
RP FUNCTION, AND INDUCTION.
RC STRAIN=168 / BR95;
RX PubMed=8825777; DOI=10.1046/j.1365-2958.1996.376903.x;
RA Glatz E., Nilsson R.P., Rutberg L., Rutberg B.;
RT "A dual role for the Bacillus subtilis glpD leader and the GlpP protein in
RT the regulated expression of glpD: antitermination and control of mRNA
RT stability.";
RL Mol. Microbiol. 19:319-328(1996).
RN [8]
RP FUNCTION, AND INDUCTION.
RC STRAIN=168 / BR95;
RX PubMed=9595668; DOI=10.1111/j.1574-6968.1998.tb12983.x;
RA Glatz E., Farewell A., Rutberg B.;
RT "The Bacillus subtilis glpD leader and antiterminator protein GlpP provide
RT a target for glucose repression in Escherichia coli.";
RL FEMS Microbiol. Lett. 162:93-96(1998).
RN [9]
RP FUNCTION.
RC STRAIN=168 / BR95;
RX PubMed=9493382; DOI=10.1099/00221287-144-2-449;
RA Glatz E., Persson M., Rutberg B.;
RT "Antiterminator protein GlpP of Bacillus subtilis binds to glpD leader
RT mRNA.";
RL Microbiology 144:449-456(1998).
CC -!- FUNCTION: Regulates expression of the glpD operon. In the presence of
CC glycerol 3-phosphate (G3P) causes antitermination of transcription of
CC glpD at the inverted repeat of the leader region to enhance its
CC transcription. Binds and stabilizes glpD leader mRNA. May also regulate
CC expression of the glpFK operon. {ECO:0000269|PubMed:1809833,
CC ECO:0000269|PubMed:182672, ECO:0000269|PubMed:4368746,
CC ECO:0000269|PubMed:8825777, ECO:0000269|PubMed:9493382,
CC ECO:0000269|PubMed:9595668}.
CC -!- INDUCTION: By glycerol 3-phosphate. Repressed by glucose, glucose 6-
CC phosphate and fructose 6-phosphate. {ECO:0000269|PubMed:8825777,
CC ECO:0000269|PubMed:9595668}.
CC -!- DISRUPTION PHENOTYPE: Defective in glycerol 3-phosphate uptake.
CC Noninducible for glpK and glpD. Is able to grow at concentrations of
CC the antibiotic fosfomycin that is not tolerated by the wild-type.
CC {ECO:0000269|PubMed:182672, ECO:0000269|PubMed:4368746}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M99611; AAA22489.1; -; Genomic_DNA.
DR EMBL; Y14079; CAA74427.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12755.1; -; Genomic_DNA.
DR PIR; B47700; B47700.
DR RefSeq; NP_388808.1; NC_000964.3.
DR RefSeq; WP_003233388.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P30300; -.
DR SMR; P30300; -.
DR STRING; 224308.BSU09270; -.
DR PaxDb; P30300; -.
DR PRIDE; P30300; -.
DR EnsemblBacteria; CAB12755; CAB12755; BSU_09270.
DR GeneID; 936251; -.
DR KEGG; bsu:BSU09270; -.
DR PATRIC; fig|224308.43.peg.969; -.
DR eggNOG; COG1954; Bacteria.
DR InParanoid; P30300; -.
DR OMA; PAIRNMK; -.
DR PhylomeDB; P30300; -.
DR BioCyc; BSUB:BSU09270-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001072; F:transcription antitermination factor activity, RNA binding; IDA:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:UniProtKB.
DR GO; GO:0006071; P:glycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0060567; P:negative regulation of DNA-templated transcription, termination; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IMP:UniProtKB.
DR GO; GO:0031564; P:transcription antitermination; IDA:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006699; GlpP.
DR PANTHER; PTHR35787; PTHR35787; 1.
DR Pfam; PF04309; G3P_antiterm; 1.
DR PIRSF; PIRSF016897; GlpP; 1.
PE 2: Evidence at transcript level;
KW Glycerol metabolism; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..192
FT /note="Glycerol uptake operon antiterminator regulatory
FT protein"
FT /id="PRO_0000087518"
SQ SEQUENCE 192 AA; 21609 MW; E3B9A85C5AFA3949 CRC64;
MMSFHNQPIL PAIRNMKQFD EFLNSSFSYG VILDIHLGQL KGVIKEAQKH GKNMMVHVDL
IQGIKHDEYG AEFICQDIKP AGIISTRSNV IAKAKQKKIY AIQRLFLLDT SAMEKSMEFI
GKHKPDFIEV LPGIVPSLIQ EIKEKTGIPI FAGGFIRTEE DVEQALKAGA VAVTTSNTKL
WKKYENFLTE SD
