PTGCB_BUCAI
ID PTGCB_BUCAI Reviewed; 477 AA.
AC P57437;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=BU356;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13060.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000003; BAB13060.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_240174.2; NC_002528.1.
DR RefSeq; WP_009874312.1; NC_002528.1.
DR AlphaFoldDB; P57437; -.
DR SMR; P57437; -.
DR STRING; 107806.10039026; -.
DR EnsemblBacteria; BAB13060; BAB13060; BAB13060.
DR KEGG; buc:BU356; -.
DR PATRIC; fig|107806.10.peg.369; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_1_0_6; -.
DR OMA; AWAFNRF; -.
DR Proteomes; UP000001806; 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; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..477
FT /note="PTS system glucose-specific EIICB component"
FT /id="PRO_0000186525"
FT TRANSMEM 15..35
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 191..211
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 357..377
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; 51727 MW; 5204C68E94477C5F CRC64;
MFKNVFANLQ KVGKSLMLPV SVLPIAGILL GIGSAHFNFL PDILSQIMAQ TGGSVFSNMP
LIFAIGVALG FTNNDGVAAL AAVVSYGILI QTLTAVEPIV LHTTIEVIKN KHLSDTGILG
GIIAGAISAY MFNKFYRIQL PEYLGFFAGK RFVPIISGLS AILIGVILSL IWPPIGHGIQ
IFSKWAAYQN PILAFALYGL VERALVPFGL HHIWNVPFQM QIGEYTNSIG QVFHGDIARY
MAGDSTAGNL SGGFIFKMYG LPGAALAIWH TSKKENKTKI GSIMISAALT AFLTGITEPI
EFSFIIVAPV LYVIHAILAG LSFPLCIFLD MRAGTSFSHG FIDFIVLSGN SHHILLFPII
GILYGLLYYI LFYLFIINFN LDTPGRENIK NNILEKDNNE IAPYIITALG GKNNIKNLDA
CITRLRITVS DISKVKQKDL KNIGAAGIII SGSGIQVVFG TRSENIKTAM DECIKNI
