PTV3B_BACSU
ID PTV3B_BACSU Reviewed; 609 AA.
AC P40739; Q45661;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=PTS system beta-glucoside-specific EIIBCA component;
DE AltName: Full=EIIBCA-Bgl;
DE Short=EII-Bgl;
DE Includes:
DE RecName: Full=Beta-glucoside-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.-;
DE AltName: Full=PTS system beta-glucoside-specific EIIB component;
DE Includes:
DE RecName: Full=Beta-glucoside permease IIC component;
DE AltName: Full=PTS system beta-glucoside-specific EIIC component;
DE Includes:
DE RecName: Full=Beta-glucoside-specific phosphotransferase enzyme IIA component;
DE AltName: Full=PTS system beta-glucoside-specific EIIA component;
GN Name=bglP; OrderedLocusNames=BSU39270; ORFNames=N17C;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7883710; DOI=10.1128/jb.177.6.1527-1535.1995;
RA Le Coq D., Lindner C., Krueger S., Steinmetz M., Stuelke J.;
RT "New beta-glucoside (bgl) genes in Bacillus subtilis: the bglP gene product
RT has both transport and regulatory functions similar to those of BglF, its
RT Escherichia coli homolog.";
RL J. Bacteriol. 177:1527-1535(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7704263; DOI=10.1099/13500872-141-2-337;
RA Yoshida K., Sano H., Seki S., Oda M., Fujimura M., Fujita Y.;
RT "Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome
RT containing the hut and wapA loci.";
RL Microbiology 141:337-343(1995).
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 SEQUENCE REVISION TO 434.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-182.
RC STRAIN=168;
RX PubMed=8628237; DOI=10.1007/bf02172988;
RA Beloin C., Hirschbein L., Le Hegarat F.;
RT "Suppression of the Bgl+ phenotype of a delta hns strain of Escherichia
RT coli by a Bacillus subtilis antiterminator binding site.";
RL Mol. Gen. Genet. 250:761-766(1996).
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 beta-glucoside transport (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC cysteinyl or histidyl residue, depending on the transported sugar.
CC Then, it transfers the phosphoryl group to the sugar substrate
CC concomitantly with the sugar uptake processed by the EIIC domain.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site.
CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC residue. Then, it transfers the phosphoryl group to the EIIB domain.
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DR EMBL; Z34526; CAA84286.1; -; Genomic_DNA.
DR EMBL; D31856; BAA06652.1; -; Genomic_DNA.
DR EMBL; D29985; BAA06256.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15963.2; -; Genomic_DNA.
DR EMBL; X85408; CAA59697.1; -; Genomic_DNA.
DR PIR; I40406; I40406.
DR PIR; T47097; T47097.
DR RefSeq; NP_391806.2; NC_000964.3.
DR RefSeq; WP_003242943.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P40739; -.
DR SMR; P40739; -.
DR STRING; 224308.BSU39270; -.
DR TCDB; 4.A.1.2.11; the pts glucose-glucoside (glc) family.
DR jPOST; P40739; -.
DR PaxDb; P40739; -.
DR PRIDE; P40739; -.
DR EnsemblBacteria; CAB15963; CAB15963; BSU_39270.
DR GeneID; 937518; -.
DR KEGG; bsu:BSU39270; -.
DR PATRIC; fig|224308.179.peg.4251; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR InParanoid; P40739; -.
DR OMA; IIMTGMH; -.
DR PhylomeDB; P40739; -.
DR BioCyc; BSUB:BSU39270-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: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:0090589; F:protein-phosphocysteine-trehalose phosphotransferase system transporter 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 GO; GO:0015771; P:trehalose transport; IBA:GO_Central.
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; IPR011297; PTS_IIABC_b_glu.
DR InterPro; IPR001996; PTS_IIB_1.
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; TIGR00830; PTBA; 1.
DR TIGRFAMs; TIGR01995; PTS-II-ABC-beta; 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 3: Inferred from homology;
KW Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..609
FT /note="PTS system beta-glucoside-specific EIIBCA component"
FT /id="PRO_0000186480"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..86
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 103..459
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 480..584
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT ACT_SITE 26
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 532
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT CONFLICT 75
FT /note="A -> S (in Ref. 5; CAA59697)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="L -> F (in Ref. 2; BAA06652/BAA06256)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="G -> E (in Ref. 1; CAA84286)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="A -> S (in Ref. 2; BAA06652/BAA06256)"
FT /evidence="ECO:0000305"
FT CONFLICT 449..450
FT /note="DG -> HR (in Ref. 2; BAA06652/BAA06256)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="I -> M (in Ref. 2; BAA06652/BAA06256)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="G -> S (in Ref. 2; BAA06652/BAA06256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 609 AA; 64478 MW; C2D45B33C5C2765A CRC64;
MDYDKLSKDI LQLVGGEENV QRVIHCMTRL RFNLHDNAKA DRSQLEQLPG VMGTNISGEQ
FQIIIGNDVP KVYQAIVRHS NLSDEKSAGS SSQKKNVLSA VFDVISGVFT PILPAIAGAG
MIKGLVALAV TFGWMAEKSQ VHVILTAVGD GAFYFLPLLL AMSAARKFGS NPYVAAAIAA
AILHPDLTAL LGAGKPISFI GLPVTAATYS STVIPILLSI WIASYVEKWI DRFTHASLKL
IVVPTFTLLI VVPLTLITVG PLGAILGEYL SSGVNYLFDH AGLVAMILLA GTFSLIIMTG
MHYAFVPIMI NNIAQNGHDY LLPAMFLANM GQAGASFAVF LRSRNKKFKS LALTTSITAL
MGITEPAMYG VNMRLKKPFA AALIGGAAGG AFYGMTGVAS YIVGGNAGLP SIPVFIGPTF
IYAMIGLVIA FAAGTAAAYL LGFEDVPSDG SQQPAVHEGS REIIHSPIKG EVKALSEVKD
GVFSAGVMGK GFAIEPEEGE VVSPVRGSVT TIFKTKHAIG ITSDQGAEIL IHIGLDTVKL
EGQWFTAHIK EGDKVAPGDP LVSFDLEQIK AAGYDVITPV IVTNTDQYSF SPVKEIGKVQ
PKEALLALS
