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 03-AUG-2022, entry version 148.
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}.
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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 AlphaFoldDB; P39816; -.
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; BSU_02350.
DR GeneID; 938418; -.
DR KEGG; bsu:BSU02350; -.
DR PATRIC; fig|224308.179.peg.241; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR InParanoid; P39816; -.
DR OMA; ETDATIM; -.
DR PhylomeDB; P39816; -.
DR BioCyc; BSUB:BSU02350-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; 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;
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 BINDING 552
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P69783"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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
