PTV3B_ECOLI
ID PTV3B_ECOLI Reviewed; 625 AA.
AC P08722; Q2M840;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 187.
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=bglF; Synonyms=bglC, bglS; OrderedLocusNames=b3722, JW3700;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3309161; DOI=10.1099/00221287-133-3-563;
RA Bramley H.F., Kornberg H.L.;
RT "Nucleotide sequence of bglC, the gene specifying enzymeIIbgl of the
RT PEP:sugar phosphotransferase system in Escherichia coli K12, and
RT overexpression of the gene product.";
RL J. Gen. Microbiol. 133:563-573(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3034860; DOI=10.1128/jb.169.6.2579-2590.1987;
RA Schnetz K., Toloczyki C., Rak B.;
RT "Beta-glucoside (bgl) operon of Escherichia coli K-12: nucleotide sequence,
RT genetic organization, and possible evolutionary relationship to regulatory
RT components of two Bacillus subtilis genes.";
RL J. Bacteriol. 169:2579-2590(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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.
CC -!- FUNCTION: Acts as both a kinase and a phosphatase on BglG.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
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.
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; M15746; AAA83837.1; -; Genomic_DNA.
DR EMBL; M16487; AAA23510.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62073.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76745.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77566.1; -; Genomic_DNA.
DR PIR; C25977; C25977.
DR RefSeq; NP_418178.1; NC_000913.3.
DR RefSeq; WP_000137296.1; NZ_STEB01000015.1.
DR AlphaFoldDB; P08722; -.
DR SMR; P08722; -.
DR BioGRID; 4262137; 5.
DR BioGRID; 852538; 1.
DR DIP; DIP-9215N; -.
DR IntAct; P08722; 1.
DR STRING; 511145.b3722; -.
DR TCDB; 4.A.1.2.2; the pts glucose-glucoside (glc) family.
DR PaxDb; P08722; -.
DR EnsemblBacteria; AAC76745; AAC76745; b3722.
DR EnsemblBacteria; BAE77566; BAE77566; BAE77566.
DR GeneID; 948236; -.
DR KEGG; ecj:JW3700; -.
DR KEGG; eco:b3722; -.
DR PATRIC; fig|1411691.4.peg.2979; -.
DR EchoBASE; EB0113; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR HOGENOM; CLU_012312_2_1_6; -.
DR InParanoid; P08722; -.
DR OMA; LWQVCVI; -.
DR PhylomeDB; P08722; -.
DR BioCyc; EcoCyc:BGLF-MON; -.
DR BioCyc; MetaCyc:BGLF-MON; -.
DR PRO; PR:P08722; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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 InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
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; TIGR00852; pts-Glc; 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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..625
FT /note="PTS system beta-glucoside-specific EIIBCA component"
FT /id="PRO_0000186481"
FT TOPO_DOM 1..99
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 121..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 162..166
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 188..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 224..244
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 266..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 306..324
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 346..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 375..380
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 402..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 425..431
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 453..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..84
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 102..465
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 495..599
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT ACT_SITE 24
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 547
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
SQ SEQUENCE 625 AA; 66483 MW; 9E12A2207125C4E6 CRC64;
MTELARKIVA GVGGADNIVS LMHCATRLRF KLKDESKAQA EVLKKTPGII MVVESGGQFQ
VVIGNHVADV FLAVNSVAGL DEKAQQAPEN DDKGNLLNRF VYVISGIFTP LIGLMAATGI
LKGMLALALT FQWTTEQSGT YLILFSASDA LFWFFPIILG YTAGKRFGGN PFTAMVIGGA
LVHPLILTAF ENGQKADALG LDFLGIPVTL LNYSSSVIPI IFSAWLCSIL ERRLNAWLPS
AIKNFFTPLL CLMVITPVTF LLVGPLSTWI SELIAAGYLW LYQAVPAFAG AVMGGFWQIF
VMFGLHWGLV PLCINNFTVL GYDTMIPLLM PAIMAQVGAA LGVFLCERDA QKKVVAGSAA
LTSLFGITEP AVYGVNLPRK YPFVIACISG ALGATIIGYA QTKVYSFGLP SIFTFMQTIP
STGIDFTVWA SVIGGVIAIG CAFVGTVMLH FITAKRQPAQ GAPQEKTPEV ITPPEQGGIC
SPMTGEIVPL IHVADTTFAS GLLGKGIAIL PSVGEVRSPV AGRIASLFAT LHAIGIESDD
GVEILIHVGI DTVKLDGKFF SAHVNVGDKV NTGDRLISFD IPAIREAGFD LTTPVLISNS
DDFTDVLPHG TAQISAGEPL LSIIR
