PTOCB_BACSU
ID PTOCB_BACSU Reviewed; 527 AA.
AC P54715;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=PTS system maltose-specific EIICB component {ECO:0000303|PubMed:16707683};
DE Includes:
DE RecName: Full=Maltose permease IIC component {ECO:0000303|PubMed:16707683};
DE AltName: Full=PTS system maltose-specific EIIC component {ECO:0000303|PubMed:16707683};
DE Includes:
DE RecName: Full=Maltose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:16707683};
DE EC=2.7.1.208 {ECO:0000269|PubMed:16707683};
DE AltName: Full=PTS system maltose-specific EIIB component {ECO:0000303|PubMed:16707683};
GN Name=malP {ECO:0000303|PubMed:16707683};
GN Synonyms=glv-2, glvC {ECO:0000303|PubMed:8704981}, glvCB, yfiB;
GN OrderedLocusNames=BSU08200;
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;
RX PubMed=8704981; DOI=10.1099/13500872-142-6-1417;
RA Yamamoto H., Uchiyama S., Fajar A.N., Ogasawara N., Sekiguchi J.;
RT "Determination of a 12 kb nucleotide sequence around the 76 degrees region
RT of the Bacillus subtilis chromosome.";
RL Microbiology 142:1417-1421(1996).
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 INDUCTION.
RX PubMed=11489864; DOI=10.1128/jb.183.17.5110-5121.2001;
RA Yamamoto H., Serizawa M., Thompson J., Sekiguchi J.;
RT "Regulation of the glv operon in Bacillus subtilis: YfiA (GlvR) is a
RT positive regulator of the operon that is repressed through CcpA and cre.";
RL J. Bacteriol. 183:5110-5121(2001).
RN [4]
RP FUNCTION IN MALTOSE UPTAKE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=16707683; DOI=10.1128/jb.00213-06;
RA Schoenert S., Seitz S., Krafft H., Feuerbaum E.-A., Andernach I., Witz G.,
RA Dahl M.K.;
RT "Maltose and maltodextrin utilization by Bacillus subtilis.";
RL J. Bacteriol. 188:3911-3922(2006).
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 is involved in maltose transport. {ECO:0000269|PubMed:16707683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-maltose(out) + N(pros)-phospho-L-histidyl-[protein] = alpha-
CC maltose 6'-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:49300, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:17306, ChEBI:CHEBI:29979, ChEBI:CHEBI:57478,
CC ChEBI:CHEBI:64837; EC=2.7.1.208;
CC Evidence={ECO:0000269|PubMed:16707683};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for maltose {ECO:0000269|PubMed:16707683};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- INDUCTION: By maltose; repressed by glucose.
CC {ECO:0000269|PubMed:11489864}.
CC -!- DOMAIN: The EIIC domain type-1 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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene show no maltose uptake.
CC {ECO:0000269|PubMed:16707683}.
CC -!- MISCELLANEOUS: Maltose uptake in B.subtilis occurs only via the malP-
CC encoded specific PTS-dependent EIICB(Mal) and not via another transport
CC mechanism. {ECO:0000305|PubMed:16707683}.
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DR EMBL; D50543; BAA09105.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12649.1; -; Genomic_DNA.
DR PIR; G69635; G69635.
DR RefSeq; NP_388701.1; NC_000964.3.
DR RefSeq; WP_003233606.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P54715; -.
DR SMR; P54715; -.
DR STRING; 224308.BSU08200; -.
DR TCDB; 4.A.1.1.8; the pts glucose-glucoside (glc) family.
DR PaxDb; P54715; -.
DR PRIDE; P54715; -.
DR EnsemblBacteria; CAB12649; CAB12649; BSU_08200.
DR GeneID; 939713; -.
DR KEGG; bsu:BSU08200; -.
DR PATRIC; fig|224308.179.peg.886; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR InParanoid; P54715; -.
DR OMA; WIPMFHN; -.
DR PhylomeDB; P54715; -.
DR BioCyc; BSUB:BSU08200-MON; -.
DR SABIO-RK; P54715; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; 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; 3.30.1360.60; -; 1.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR InterPro; IPR010975; PTS_IIBC_a_glc.
DR InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR00852; pts-Glc; 1.
DR TIGRFAMs; TIGR02005; PTS-IIBC-alpha; 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 1: Evidence at protein level;
KW Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..527
FT /note="PTS system maltose-specific EIICB component"
FT /id="PRO_0000186582"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..418
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 449..527
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 471
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 527 AA; 58055 MW; D708C38048D4D63C CRC64;
MMQKIQRFGS AMFVPVLLFA FAGIIVGIST LFKNKTLMGP LADPDGFWYQ CWYIIEQGGW
TVFNQMPLLF AIGIPVALAK KAQARACLEA LTVYLTFNYF VSAILTVWGG AFGVDMNQEV
GGTSGLTMIA GIKTLDTNII GAIFISSIVV FLHNRYFDKK LPDFLGIFQG STYIVMISFF
IMIPIALAVS YIWPMVQSGI GSLQSFLVAS GAVGVWIYTF LERILIPTGL HHFIYTPFIY
GPAVAEGGIV TYWAQHLGEY SQSAKPLKEL FPQGGFALHG NSKIFGIPGI ALAFYVTAKK
EKKKLVAGLL IPVTLTAIVA GITEPIEFTF LFISPFLFAV HAVLAATMST VMYMAGVVGN
MGGGLIEAVT LNWIPLFGSH GMTYVYQILI GLSFTAIYFF VFRFLILKFN IATPGREKDE
QQETKLYSKK EYRERKNKDE TASAAETADD TAFLYIEALG GKDNITEVTN CATRLRVSVK
DETKVEPDSV FRALGAHGVV RNGKAFQVII GLSVPQMRER VEKILNQ
