(data stored in SCRATCH zone)

SWISSPROT: PTW3C_BACSU

ID   PTW3C_BACSU             Reviewed;         631 AA.
AC   P39816;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   11-DEC-2019, entry version 141.
DE   RecName: Full=Putative PTS system glucosamine-specific EIICBA component {ECO:0000303|PubMed:10627040};
DE   Includes:
DE     RecName: Full=Glucosamine permease IIC component {ECO:0000303|PubMed:10627040};
DE     AltName: Full=PTS system glucosamine-specific EIIC component {ECO:0000303|PubMed:10627040};
DE   Includes:
DE     RecName: Full=Glucosamine-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P09323};
DE              EC=2.7.1.193 {ECO:0000250|UniProtKB:P09323};
DE     AltName: Full=PTS system glucosamine-specific EIIB component {ECO:0000250|UniProtKB:P09323};
DE   Includes:
DE     RecName: Full=Glucosamine-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P09323};
DE     AltName: Full=PTS system glucosamine-specific EIIA component {ECO:0000250|UniProtKB:P09323};
GN   Name=gamP {ECO:0000303|PubMed:10627040}; Synonyms=ybfS, yzfA;
GN   OrderedLocusNames=BSU02350;
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;
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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 515-631.
RC   STRAIN=168 / 6GM;
RX   PubMed=7751298; DOI=10.1128/jb.177.10.2863-2869.1995;
RA   Tolner B., Ubbink-Kok T., Poolman B., Konings W.N.;
RT   "Characterization of the proton/glutamate symport protein of Bacillus
RT   subtilis and its functional expression in Escherichia coli.";
RL   J. Bacteriol. 177:2863-2869(1995).
RN   [4]
RP   GENE NAME, AND PUTATIVE FUNCTION.
RX   PubMed=10627040; DOI=10.1099/00221287-145-12-3419;
RA   Reizer J., Bachem S., Reizer A., Arnaud M., Saier M.H. Jr., Stuelke J.;
RT   "Novel phosphotransferase system genes revealed by genome analysis - the
RT   complete complement of PTS proteins encoded within the genome of Bacillus
RT   subtilis.";
RL   Microbiology 145:3419-3429(1999).
RN   [5]
RP   INDUCTION.
RX   PubMed=24673833; DOI=10.1111/mmi.12544;
RA   Gaugue I., Oberto J., Plumbridge J.;
RT   "Regulation of amino sugar utilization in Bacillus subtilis by the GntR
RT   family regulators, NagR and GamR.";
RL   Mol. Microbiol. 92:100-115(2014).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane. This
CC       system may be involved in glucosamine transport.
CC       {ECO:0000250|UniProtKB:P09323, ECO:0000305|PubMed:10627040}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-
CC         glucosamine(out) = L-histidyl-[protein] + N-acetyl-D-glucosamine 6-
CC         phosphate(in); Xref=Rhea:RHEA:49240, Rhea:RHEA-COMP:9745, Rhea:RHEA-
CC         COMP:9746, ChEBI:CHEBI:29979, ChEBI:CHEBI:57513, ChEBI:CHEBI:64837,
CC         ChEBI:CHEBI:506227; EC=2.7.1.193;
CC         Evidence={ECO:0000250|UniProtKB:P09323};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P69783};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}.
CC   -!- INDUCTION: Expression is repressed by the HTH-type transcriptional
CC       regulator GamR. {ECO:0000269|PubMed:24673833}.
CC   -!- DOMAIN: The PTS EIIC type-1 domain forms the PTS system translocation
CC       channel and contains the specific substrate-binding site.
CC       {ECO:0000255|PROSITE-ProRule:PRU00426}.
CC   -!- DOMAIN: The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA on
CC       a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC       sugar substrate concomitantly with the sugar uptake processed by the
CC       PTS EIIC type-1 domain. {ECO:0000255|PROSITE-ProRule:PRU00421}.
CC   -!- DOMAIN: The PTS EIIA type-1 domain is phosphorylated by phospho-HPr on
CC       a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC       EIIB type-1 domain. {ECO:0000255|PROSITE-ProRule:PRU00416}.
DR   EMBL; AB006424; BAA33132.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12029.1; -; Genomic_DNA.
DR   EMBL; U15147; AAA82877.1; -; Genomic_DNA.
DR   PIR; D69750; D69750.
DR   RefSeq; NP_388117.1; NC_000964.3.
DR   RefSeq; WP_003246270.1; NZ_JNCM01000030.1.
DR   SMR; P39816; -.
DR   STRING; 224308.BSU02350; -.
DR   TCDB; 4.A.1.1.6; the pts glucose-glucoside (glc) family.
DR   PaxDb; P39816; -.
DR   PRIDE; P39816; -.
DR   EnsemblBacteria; CAB12029; CAB12029; BSU02350.
DR   GeneID; 938418; -.
DR   KEGG; bsu:BSU02350; -.
DR   PATRIC; fig|224308.179.peg.241; -.
DR   eggNOG; ENOG4108IIZ; Bacteria.
DR   eggNOG; COG2190; LUCA.
DR   HOGENOM; HOG000250993; -.
DR   InParanoid; P39816; -.
DR   KO; K02763; -.
DR   KO; K02764; -.
DR   KO; K02765; -.
DR   OMA; DFCIRRF; -.
DR   PhylomeDB; P39816; -.
DR   BioCyc; BSUB:BSU02350-MONOMER; -.
DR   Proteomes; UP000001570; 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:0005355; F:glucose transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   Gene3D; 2.70.70.10; -; 1.
DR   Gene3D; 3.30.1360.60; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR001127; PTS_EIIA_1_perm.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   InterPro; IPR011299; PTS_IIBC_glc.
DR   Pfam; PF00358; PTS_EIIA_1; 1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
DR   SUPFAM; SSF55604; SSF55604; 1.
DR   TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR   TIGRFAMs; TIGR00830; PTBA; 1.
DR   TIGRFAMs; TIGR02002; PTS-II-BC-glcB; 1.
DR   PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR   PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR   PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P39816.
DR   SWISS-2DPAGE; P39816.
KW   Cell membrane; Kinase; Membrane; Metal-binding; Phosphoprotein;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transmembrane; Transmembrane helix; Transport; Zinc.
FT   CHAIN           1..631
FT                   /note="Putative PTS system glucosamine-specific EIICBA
FT                   component"
FT                   /id="PRO_0000186710"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          1..382
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          397..478
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   DOMAIN          515..619
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   ACT_SITE        419
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   ACT_SITE        567
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   METAL           552
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   METAL           567
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   SITE            552
FT                   /note="Important for phospho-donor activity"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   MOD_RES         419
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000250|UniProtKB:P69786, ECO:0000305"
FT   MOD_RES         567
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P69786, ECO:0000305"
SQ   SEQUENCE   631 AA;  68145 MW;  88388A72EEC85B9B CRC64;
     MFKKAFQILQ QLGRALMTPV AVLPAAGLLL RFGDKDLLNI PIIKDAGGVV FDNLPLIFAV
     GVAIGLAGGE GVAGLAAVIG YLILTVTLDN MGKLLGLQPP YEGAEHLIDM GVFGGIIIGL
     LAAYLYKRFS SIELHPVLGF FSGKRFVPII TSVSSLVIGV IFSFVWPLIQ NGINAASSLI
     ADSTVGLFFY ATIYRLLIPF GLHHIFYTPF YFMMGEYTDP STGNTVTGDL TRFFAGDPTA
     GRFMMGDFPY MIFCLPAVAL AIIHTARPEK KKMISGVMIS AALTSMLTGI TEPVEFSFLF
     VAPVLYLINS ILAGVIFVVC DLFHVRHGYT FSGGGIDYVL NYGLSTNGWV VIPVGIVFAF
     IYYYLFRFAI LKWNLKTPGR ETDEDGQNEE KAPVAKDQLA FHVLQALGGQ QNIANLDACI
     TRLRVTVHQP SQVCKDELKR LGAVGVLEVN NNFQAIFGTK SDALKDDIKT IMAGGVPATA
     AALDTVTDKP LKPDSDETFI YPIKGETVSL GDVPDQVFSE KMMGEGFAII PSEGKVVAPA
     DGEIVSIFPT KHAIGFMSAG GTEILIHVGI DTVKLNGEGF EAHVTSGQAV KQGELLLTFD
     LNYIKQHAAS AITPVIFTNT SEEDLKHIQM K
//

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