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PTXB_ECOLI
ID   PTXB_ECOLI              Reviewed;         161 AA.
AC   P69789; A0A385XNH2; P31451; Q2M7Z4;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Phosphotransferase enzyme IIB component GlvB;
DE            EC=2.7.1.-;
DE   AltName: Full=PTS system EIIB component;
GN   Name=glvB {ECO:0000303|PubMed:8019415}; Synonyms=glvC, yidN;
GN   OrderedLocusNames=b3682, JW3659;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
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   [2]
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   [3]
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   [4]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=8019415; DOI=10.1002/pro.5560030309;
RA   Reizer J., Michotey V., Reizer A., Saier M.H. Jr.;
RT   "Novel phosphotransferase system genes revealed by bacterial genome
RT   analysis: unique, putative fructose- and glucoside-specific systems.";
RL   Protein Sci. 3:440-450(1994).
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       operon may be cryptic in wild-type K12 strains (Probable).
CC       {ECO:0000250, ECO:0000305|PubMed:8019415}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
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.
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DR   EMBL; L10328; AAA62034.1; -; Genomic_DNA.
DR   EMBL; U00096; AYC08252.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77612.1; -; Genomic_DNA.
DR   PIR; C65170; C65170.
DR   RefSeq; WP_000492410.1; NZ_CP047127.1.
DR   AlphaFoldDB; P69789; -.
DR   SMR; P69789; -.
DR   IntAct; P69789; 2.
DR   STRING; 316407.85676362; -.
DR   PRIDE; P69789; -.
DR   EnsemblBacteria; AYC08252; AYC08252; b3682.
DR   EnsemblBacteria; BAE77612; BAE77612; BAE77612.
DR   KEGG; ecj:JW3659; -.
DR   PATRIC; fig|83333.103.peg.4617; -.
DR   EchoBASE; EB1660; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   HOGENOM; CLU_012312_8_1_6; -.
DR   PhylomeDB; P69789; -.
DR   BioCyc; EcoCyc:GLVB-MON; -.
DR   PRO; PR:P69789; -.
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; IEA:UniProtKB-SubCell.
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; IPR001996; PTS_IIB_1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   SUPFAM; SSF55604; SSF55604; 1.
DR   TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR   PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..161
FT                   /note="Phosphotransferase enzyme IIB component GlvB"
FT                   /id="PRO_0000186580"
FT   TRANSMEM        10..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          70..152
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   ACT_SITE        92
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   161 AA;  17626 MW;  CB73C19B7C3CA41D CRC64;
     MFSNHADMML TQIAIGLCFT LLYFVVFRTL ILQFNMCTPG REDAEVKLYS KAEYKASRGQ
     TTAAEPKKEL DQAAGILQAL GGVGNISSIN NCATRLRIAL HDMSQTLDDE VFKKLGAHGV
     FRSGDAIQVI IGLHVSQLRE QLDSLINSHQ SAENVAITEA V
 
 
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