PTGCB_BUCBP
ID PTGCB_BUCBP Reviewed; 479 AA.
AC Q89AG6;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=bbp_326;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27048.1; -; Genomic_DNA.
DR RefSeq; WP_011091449.1; NC_004545.1.
DR AlphaFoldDB; Q89AG6; -.
DR SMR; Q89AG6; -.
DR STRING; 224915.bbp_326; -.
DR EnsemblBacteria; AAO27048; AAO27048; bbp_326.
DR GeneID; 56470865; -.
DR KEGG; bab:bbp_326; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_1_0_6; -.
DR OMA; AWAFNRF; -.
DR OrthoDB; 2035550at2; -.
DR Proteomes; UP000000601; 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..479
FT /note="PTS system glucose-specific EIICB component"
FT /id="PRO_0000186527"
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 80..100
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 252..272
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 305..325
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 356..376
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..479
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 479 AA; 52157 MW; FF1B60760B4D9ABD CRC64;
MFKNAFSNLQ KIGRSLMLPV SVLPIAGILL GIGSANFKII PHTISNIMTE AGSSVFSNMP
LIFAIGIALG FTKNDGVSAL AAVVSYGIMT KTLSITIPIF SNLSDINVNQ KYLLDTGILG
GIIAGSISAY IFNTFYRIQL PEYLGFFAGR RFVPIASGLI SIIFGCILSI IWPPIGNVIK
TFSEWAAYQN PTLAFGIYGT VERALVPFGL HHIWNVPFQM QIGEYNNSIG QIFHGDIARY
MAGDSTAGKL SGGFIFKMYG LPFAALAMWH CANKKNKAKI GGIMMSGALT AILTGITEPI
EFSFILVAPI LYVIHAILAG LAFPICILLN MRSGTSFSHG LIDFIVLSGN SNNFWLFPIV
GLFYGILYYG IFYFMIKKFN LKTPGREKSI TYINQKTIKE TALLVISILG GKTNIINLDA
CITRLRITVL DISKVNQKKL KNLGASGVIV SGSGIQIVFG TQSDHIKTEI DNYMSNTNQ
