PTQB_ECOLI
ID PTQB_ECOLI Reviewed; 106 AA.
AC P69795; P17409;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=PTS system N,N'-diacetylchitobiose-specific EIIB component {ECO:0000303|PubMed:2092358};
DE AltName: Full=EIIB-Chb {ECO:0000303|PubMed:2092358};
DE AltName: Full=IVcel {ECO:0000303|PubMed:2092358};
DE AltName: Full=N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:2092358};
DE EC=2.7.1.196 {ECO:0000269|PubMed:10913117, ECO:0000269|PubMed:10913119};
GN Name=chbB {ECO:0000303|PubMed:9405618};
GN Synonyms=celA {ECO:0000303|PubMed:2179047};
GN OrderedLocusNames=b1738, JW1727;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
RC STRAIN=K12;
RX PubMed=2179047; DOI=10.1093/genetics/124.3.455;
RA Parker L.L., Hall B.G.;
RT "Characterization and nucleotide sequence of the cryptic cel operon of
RT Escherichia coli K12.";
RL Genetics 124:455-471(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND ACTIVE SITE.
RX PubMed=2092358; DOI=10.1016/0923-2508(90)90079-6;
RA Reizer J., Reizer A., Saier M.H. Jr.;
RT "The cellobiose permease of Escherichia coli consists of three proteins and
RT is homologous to the lactose permease of Staphylococcus aureus.";
RL Res. Microbiol. 141:1061-1067(1990).
RN [6]
RP IDENTIFICATION OF CHB OPERON.
RX PubMed=9405618; DOI=10.1073/pnas.94.26.14367;
RA Keyhani N.O., Roseman S.;
RT "Wild-type Escherichia coli grows on the chitin disaccharide, N,N'-
RT diacetylchitobiose, by expressing the cel operon.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14367-14371(1997).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=10913117; DOI=10.1074/jbc.m001043200;
RA Keyhani N.O., Wang L.-X., Lee Y.C., Roseman S.;
RT "The chitin disaccharide, N,N'-diacetylchitobiose, is catabolized by
RT Escherichia coli and is transported/phosphorylated by the
RT phosphoenolpyruvate:glycose phosphotransferase system.";
RL J. Biol. Chem. 275:33084-33090(2000).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-10, ACTIVE SITE, AND
RP SUBUNIT.
RX PubMed=10913119; DOI=10.1074/jbc.m001045200;
RA Keyhani N.O., Bacia K., Roseman S.;
RT "The transport/phosphorylation of N,N'-diacetylchitobiose in Escherichia
RT coli. Characterization of phospho-IIB(Chb) and of a potential transition
RT state analogue in the phosphotransfer reaction between the proteins
RT IIA(Chb) and IIB(Chb).";
RL J. Biol. Chem. 275:33102-33109(2000).
RN [9]
RP MUTAGENESIS OF CYS-10, ACTIVE SITE, AND SUBUNIT.
RX PubMed=10913122; DOI=10.1074/jbc.m001717200;
RA Keyhani N.O., Rodgers M.E., Demeler B., Hansen J.C., Roseman S.;
RT "Analytical sedimentation of the IIAChb and IIBChb proteins of the
RT Escherichia coli N,N'-diacetylchitobiose phosphotransferase system.
RT Demonstration of a model phosphotransfer transition state complex.";
RL J. Biol. Chem. 275:33110-33115(2000).
RN [10]
RP STRUCTURE BY NMR, AND ACTIVE SITE.
RX PubMed=8003964; DOI=10.1002/pro.5560030212;
RA Ab E., Schuurman-Wolters G.K., Saier M.H. Jr., Reizer J., Jacuinod M.,
RA Roepstorff P., Dijkstra K., Scheek R.M., Robillard G.T.;
RT "Enzyme IIBcellobiose of the phosphoenol-pyruvate-dependent
RT phosphotransferase system of Escherichia coli: backbone assignment and
RT secondary structure determined by three-dimensional NMR spectroscopy.";
RL Protein Sci. 3:282-290(1994).
RN [11]
RP STRUCTURE BY NMR OF MUTANT SER-10, AND ACTIVE SITE.
RX PubMed=9041631; DOI=10.1002/pro.5560060205;
RA Ab E., Schuurman-Wolters G.K., Reizer J., Saier M.H. Jr., Dijkstra K.,
RA Scheek R.M., Robillard G.T.;
RT "The NMR side-chain assignments and solution structure of enzyme
RT IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase
RT system of Escherichia coli.";
RL Protein Sci. 6:304-314(1997).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT SER-10, AND ACTIVE SITE.
RX PubMed=9032081; DOI=10.1016/s0969-2126(97)00180-9;
RA van Montfort R.L.M., Pijning T., Kalk K.H., Reizer J., Saier M.H. Jr.,
RA Thunnissen M.M.G.M., Robillard G.T., Dijkstra B.W.;
RT "The structure of an energy-coupling protein from bacteria, IIBcellobiose,
RT reveals similarity to eukaryotic protein tyrosine phosphatases.";
RL Structure 5:217-225(1997).
RN [13]
RP STRUCTURE BY NMR, AND PHOSPHORYLATION AT CYS-10.
RX PubMed=11352587; DOI=10.1006/jmbi.2001.4623;
RA Ab E., Schuurman-Wolters G.K., Nijlant D., Dijkstra K., Saier M.H.,
RA Robillard G.T., Scheek R.M.;
RT "NMR structure of cysteinyl-phosphorylated enzyme IIB of the N,N'-
RT diacetylchitobiose-specific phosphoenolpyruvate-dependent
RT phosphotransferase system of Escherichia coli.";
RL J. Mol. Biol. 308:993-1009(2001).
RN [14]
RP STRUCTURE BY NMR OF 3-105 OF MUTANT SER-10, ACTIVE SITE, AND SUBUNIT.
RX PubMed=19959833; DOI=10.1074/jbc.m109.080937;
RA Jung Y.S., Cai M., Clore G.M.;
RT "Solution structure of the IIAChitobiose-IIBChitobiose complex of the N,N'-
RT diacetylchitobiose branch of the Escherichia coli phosphotransferase
RT system.";
RL J. Biol. Chem. 285:4173-4184(2010).
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 ChbABC PTS system is involved in the transport of the chitin
CC disaccharide N,N'-diacetylchitobiose (GlcNAc2) (PubMed:10913117). Also
CC able to use N,N',N''-triacetyl chitotriose (GlcNAc3) (PubMed:10913117,
CC PubMed:10913119). {ECO:0000269|PubMed:10913117,
CC ECO:0000269|PubMed:10913119, ECO:0000305|PubMed:2092358}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(pros)-phospho-L-histidyl-[protein] + N,N'-
CC diacetylchitobiose(out) = diacetylchitobiose-6'-phosphate(in) + L-
CC histidyl-[protein]; Xref=Rhea:RHEA:33423, Rhea:RHEA-COMP:9745,
CC Rhea:RHEA-COMP:9746, ChEBI:CHEBI:28681, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:64837, ChEBI:CHEBI:64883; EC=2.7.1.196;
CC Evidence={ECO:0000269|PubMed:10913117, ECO:0000269|PubMed:10913119};
CC -!- SUBUNIT: Forms a complex with ChbA (EIIA) (PubMed:10913119,
CC PubMed:10913122, PubMed:19959833). ChbB is a monomer in both its
CC unphosphorylated and phosphorylated forms (PubMed:10913122).
CC {ECO:0000269|PubMed:10913119, ECO:0000269|PubMed:10913122,
CC ECO:0000269|PubMed:19959833}.
CC -!- INTERACTION:
CC P69795; P69791: chbA; NbExp=2; IntAct=EBI-1128186, EBI-1121924;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By GlcNAc2, GlcNAc3 and beta-N,N'-diacetylchitobiose (Me-
CC TCB). {ECO:0000269|PubMed:10913117}.
CC -!- DOMAIN: The PTS EIIB type-3 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00423}.
CC -!- CAUTION: Was originally (PubMed:2092358) characterized as part of a
CC cryptic cel operon for a cellobiose degradation system. The Cel+
CC phenotype is due to mutations making expression chitobiose-independent
CC and altering the substrate specificity. {ECO:0000305|PubMed:2092358}.
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DR EMBL; X52890; CAA37069.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74808.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15519.1; -; Genomic_DNA.
DR PIR; S10870; S10870.
DR RefSeq; NP_416252.1; NC_000913.3.
DR RefSeq; WP_000412169.1; NZ_STEB01000009.1.
DR PDB; 1E2B; NMR; -; A=1-106.
DR PDB; 1H9C; NMR; -; A=1-106.
DR PDB; 1IIB; X-ray; 1.80 A; A/B=1-106.
DR PDB; 2WWV; NMR; -; D=3-105.
DR PDB; 2WY2; NMR; -; D=3-105.
DR PDBsum; 1E2B; -.
DR PDBsum; 1H9C; -.
DR PDBsum; 1IIB; -.
DR PDBsum; 2WWV; -.
DR PDBsum; 2WY2; -.
DR AlphaFoldDB; P69795; -.
DR BMRB; P69795; -.
DR SMR; P69795; -.
DR BioGRID; 4260316; 17.
DR ComplexPortal; CPX-4683; N,N'-diacetylchitobiose-specific enzyme II complex.
DR IntAct; P69795; 2.
DR STRING; 511145.b1738; -.
DR DrugBank; DB03544; S-Phosphocysteine.
DR TCDB; 4.A.3.2.1; the pts lactose-n,n'-diacetylchitobiose-Beta-glucoside (lac) family.
DR iPTMnet; P69795; -.
DR jPOST; P69795; -.
DR PaxDb; P69795; -.
DR PRIDE; P69795; -.
DR EnsemblBacteria; AAC74808; AAC74808; b1738.
DR EnsemblBacteria; BAA15519; BAA15519; BAA15519.
DR GeneID; 67415558; -.
DR GeneID; 945339; -.
DR KEGG; ecj:JW1727; -.
DR KEGG; eco:b1738; -.
DR PATRIC; fig|1411691.4.peg.518; -.
DR EchoBASE; EB0138; -.
DR eggNOG; COG1440; Bacteria.
DR HOGENOM; CLU_147323_2_0_6; -.
DR InParanoid; P69795; -.
DR OMA; DAEIFAC; -.
DR PhylomeDB; P69795; -.
DR BioCyc; EcoCyc:CELA-MON; -.
DR BioCyc; MetaCyc:CELA-MON; -.
DR BRENDA; 2.7.1.196; 2026.
DR EvolutionaryTrace; P69795; -.
DR PRO; PR:P69795; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
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:0090566; F:protein-phosphocysteine-N,N'-diacetylchitobiose phosphotransferase system transporter activity; IDA:EcoCyc.
DR GO; GO:1902815; P:N,N'-diacetylchitobiose import; IDA:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR013012; PTS_EIIB_3.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR TIGRFAMs; TIGR00853; pts-lac; 1.
DR PROSITE; PS51100; PTS_EIIB_TYPE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..106
FT /note="PTS system N,N'-diacetylchitobiose-specific EIIB
FT component"
FT /id="PRO_0000186489"
FT DOMAIN 3..106
FT /note="PTS EIIB type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT ACT_SITE 10
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000269|PubMed:10913119,
FT ECO:0000269|PubMed:10913122, ECO:0000305|PubMed:19959833,
FT ECO:0000305|PubMed:2092358, ECO:0000305|PubMed:8003964,
FT ECO:0000305|PubMed:9032081, ECO:0000305|PubMed:9041631"
FT MOD_RES 10
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423,
FT ECO:0000305|PubMed:11352587"
FT MUTAGEN 10
FT /note="C->S: Unable to be phosphorylated by EIIA."
FT /evidence="ECO:0000269|PubMed:10913119,
FT ECO:0000269|PubMed:10913122"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1IIB"
FT HELIX 13..29
FT /evidence="ECO:0007829|PDB:1IIB"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1IIB"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1IIB"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:1IIB"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1IIB"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:1IIB"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:1IIB"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1E2B"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1IIB"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:1IIB"
FT HELIX 89..104
FT /evidence="ECO:0007829|PDB:1IIB"
SQ SEQUENCE 106 AA; 11427 MW; DE4AADE300D18F53 CRC64;
MEKKHIYLFC SAGMSTSLLV SKMRAQAEKY EVPVIIEAFP ETLAGEKGQN ADVVLLGPQI
AYMLPEIQRL LPNKPVEVID SLLYGKVDGL GVLKAAVAAI KKAAAN
