PTGCB_BUCAP
ID PTGCB_BUCAP Reviewed; 477 AA.
AC Q8K9J0;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=PTS system glucose-specific EIICB component {ECO:0000250|UniProtKB:P69786};
DE AltName: Full=EIICB-Glc {ECO:0000250|UniProtKB:P69786};
DE Short=EII-Glc {ECO:0000250|UniProtKB:P69786};
DE Includes:
DE RecName: Full=Glucose permease IIC component {ECO:0000250|UniProtKB:P69786};
DE AltName: Full=PTS system glucose-specific EIIC component {ECO:0000250|UniProtKB:P69786};
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P69786};
DE EC=2.7.1.199 {ECO:0000250|UniProtKB:P69786};
DE AltName: Full=PTS system glucose-specific EIIB component {ECO:0000250|UniProtKB:P69786};
GN Name=ptsG; OrderedLocusNames=BUsg_344;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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. The
CC enzyme II complex composed of PtsG and Crr is involved in glucose
CC transport. {ECO:0000250|UniProtKB:P69786}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC glucose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:33367,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:61548, ChEBI:CHEBI:64837;
CC EC=2.7.1.199; Evidence={ECO:0000250|UniProtKB:P69786};
CC -!- SUBCELLULAR LOCATION: Cell inner 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 {ECO:0000255|PROSITE-ProRule:PRU00421}.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site. {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
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DR EMBL; AE013218; AAM67898.1; -; Genomic_DNA.
DR RefSeq; WP_011053865.1; NC_004061.1.
DR AlphaFoldDB; Q8K9J0; -.
DR SMR; Q8K9J0; -.
DR STRING; 198804.BUsg_344; -.
DR EnsemblBacteria; AAM67898; AAM67898; BUsg_344.
DR KEGG; bas:BUsg_344; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_1_0_6; -.
DR OMA; AWAFNRF; -.
DR OrthoDB; 2035550at2; -.
DR Proteomes; UP000000416; 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: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 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; IPR011299; PTS_IIBC_glc.
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; TIGR02002; PTS-II-BC-glcB; 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 inner membrane; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..477
FT /note="PTS system glucose-specific EIICB component"
FT /id="PRO_0000186526"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..388
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 399..477
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 421
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P69786,
FT ECO:0000255|PROSITE-ProRule:PRU00421"
FT MOD_RES 421
FT /note="Phosphocysteine"
FT /evidence="ECO:0000250|UniProtKB:P69786"
SQ SEQUENCE 477 AA; 51941 MW; 84CA2ABDFEA4CFA2 CRC64;
MFKNVFSSLQ KVGKSLMLPV SVLPIAGILL GIGSAHFTLI PEIISQIMAQ TGGSIFSNMP
LIFAIGVALG FSNNDGVAAL AAVVAYSILI QTLSAVELNI LNTDANTIKN KNFSDIGILG
GIIAGAISAY MFNKFYKIQL PEYLGFFAGK RFVPIISGLF AIFVGLILSL IWPSIGNKIQ
IFSEWAAYQN PIIAFSLYGL VERALVPFGL HHIWNVPFQM QIGEYKNSIG QIFHGDIARY
MAGDTTAGNL SGGFIFKMYG LPGAALAIWH TAKKENRKKI GSIMISAALT AFLTGITEPI
EFSFILVAPI LYIIHAILAG LSFPLCIFLN MRAGTSFSHG FIDFIVLSGH SHKIFLFPIV
GICYGLLYYS IFYFLITTFN LKTPGREENK NTVFFRNNIE IAPYIVEALG GKNNIKNLDA
CITRLRITVS EISKVNEENL KNLGAAGVVI SGSGVQAVFG TRSENIKTAI DEYINNI
