PTQA_ECOLI
ID PTQA_ECOLI Reviewed; 116 AA.
AC P69791; P17335; Q47092; Q47093; Q47094; Q57128;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=PTS system N,N'-diacetylchitobiose-specific EIIA component {ECO:0000303|PubMed:2092358};
DE AltName: Full=EIIA-Chb {ECO:0000303|PubMed:2092358};
DE AltName: Full=EIII-Chb {ECO:0000303|PubMed:2179047};
DE AltName: Full=IIIcel {ECO:0000303|PubMed:2179047};
DE AltName: Full=N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:2092358};
GN Name=chbA {ECO:0000303|PubMed:9405618};
GN Synonyms=celC {ECO:0000303|PubMed:2179047};
GN OrderedLocusNames=b1736, JW1725;
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 [GENOMIC DNA].
RC STRAIN=28, 35, 37, 50, 51, 58, 6, 61, 66, 69, and ECOR 1;
RX PubMed=1630305; DOI=10.1093/oxfordjournals.molbev.a040751;
RA Hall B.G., Sharp P.M.;
RT "Molecular population genetics of Escherichia coli: DNA sequence diversity
RT at the celC, crr, and gutB loci of natural isolates.";
RL Mol. Biol. Evol. 9:654-665(1992).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND PHOSPHORYLATION AT
RP HIS-89.
RX PubMed=10913118; DOI=10.1074/jbc.m001044200;
RA Keyhani N.O., Boudker O., Roseman S.;
RT "Isolation and characterization of IIAChb, a soluble protein of the enzyme
RT II complex required for the transport/phosphorylation of N, N'-
RT diacetylchitobiose in Escherichia coli.";
RL J. Biol. Chem. 275:33091-33101(2000).
RN [10]
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 [11]
RP 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 [12]
RP STRUCTURE BY NMR OF 14-116 OF MUTANT LEU-92, MUTAGENESIS OF ASP-92,
RP COFACTOR, ACTIVE SITE, SUBUNIT, AND PHOSPHORYLATION AT HIS-89.
RX PubMed=15654077; DOI=10.1074/jbc.m414300200;
RA Tang C., Williams D.C. Jr., Ghirlando R., Clore G.M.;
RT "Solution structure of enzyme IIA(Chitobiose) from the N,N'-
RT diacetylchitobiose branch of the Escherichia coli phosphotransferase
RT system.";
RL J. Biol. Chem. 280:11770-11780(2005).
RN [13]
RP STRUCTURE BY NMR OF 14-116 OF MUTANT GLU-89, 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).
RN [14]
RP STRUCTURE BY NMR OF 14-116 OF MUTANT GLU-89 IN COMPLEX WITH THE HISTIDINE
RP PHOSPHOCARRIER PROTEIN HPR, ACTIVE SITE, SUBUNIT, AND PHOSPHORYLATION AT
RP HIS-89.
RX PubMed=22593574; DOI=10.1074/jbc.m112.371492;
RA Jung Y.S., Cai M., Clore G.M.;
RT "Solution structure of the IIAChitobiose-HPr complex of the N,N'-
RT diacetylchitobiose branch of the Escherichia coli phosphotransferase
RT system.";
RL J. Biol. Chem. 287:23819-23829(2012).
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:10913118,
CC PubMed:10913117). Also able to use N,N',N''-triacetyl chitotriose
CC (GlcNAc3) (PubMed:10913117). {ECO:0000269|PubMed:10913117,
CC ECO:0000269|PubMed:10913118, ECO:0000305|PubMed:2092358}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10913118, ECO:0000305|PubMed:15654077};
CC Note=Can also use copper and nickel with lower efficiency.
CC {ECO:0000269|PubMed:10913118};
CC -!- SUBUNIT: Forms a complex with ChbB (EIIB) (PubMed:10913119,
CC PubMed:10913122, PubMed:19959833). ChbA is a homotrimer
CC (PubMed:10913122, PubMed:15654077, PubMed:19959833, PubMed:22593574).
CC The interface of the homotrimer is stabilized by metal cations such as
CC magnesium, copper or nickel (PubMed:15654077).
CC {ECO:0000269|PubMed:10913119, ECO:0000269|PubMed:10913122,
CC ECO:0000269|PubMed:15654077, ECO:0000269|PubMed:19959833,
CC ECO:0000269|PubMed:22593574, ECO:0000305|PubMed:10913118}.
CC -!- INTERACTION:
CC P69791; P69795: chbB; NbExp=2; IntAct=EBI-1121924, EBI-1128186;
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 EIIA type-3 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00418}.
CC -!- CAUTION: Was originally (PubMed:2179047) 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:2179047}.
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DR EMBL; X52890; CAA37071.1; -; Genomic_DNA.
DR EMBL; M93570; AAA23551.1; -; Genomic_DNA.
DR EMBL; M93571; AAA23553.1; -; Genomic_DNA.
DR EMBL; M93572; AAA23554.1; -; Genomic_DNA.
DR EMBL; M93573; AAA23559.1; -; Genomic_DNA.
DR EMBL; M93574; AAA23556.1; -; Genomic_DNA.
DR EMBL; M93575; AAA23552.1; -; Genomic_DNA.
DR EMBL; M93576; AAA23560.1; -; Genomic_DNA.
DR EMBL; M93577; AAA23557.1; -; Genomic_DNA.
DR EMBL; M93591; AAA23561.1; -; Genomic_DNA.
DR EMBL; M93592; AAA23555.1; -; Genomic_DNA.
DR EMBL; M93593; AAA23558.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74806.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15517.1; -; Genomic_DNA.
DR PIR; H64932; H64932.
DR RefSeq; NP_416250.1; NC_000913.3.
DR RefSeq; WP_000968919.1; NZ_STEB01000009.1.
DR PDB; 1WCR; NMR; -; A/B/C=14-116.
DR PDB; 2LRK; NMR; -; A/B/C=14-116.
DR PDB; 2LRL; NMR; -; A/B/C=14-116.
DR PDB; 2WWV; NMR; -; A/B/C=14-116.
DR PDB; 2WY2; NMR; -; A/B/C=14-116.
DR PDBsum; 1WCR; -.
DR PDBsum; 2LRK; -.
DR PDBsum; 2LRL; -.
DR PDBsum; 2WWV; -.
DR PDBsum; 2WY2; -.
DR AlphaFoldDB; P69791; -.
DR BMRB; P69791; -.
DR SMR; P69791; -.
DR BioGRID; 4259134; 12.
DR ComplexPortal; CPX-4683; N,N'-diacetylchitobiose-specific enzyme II complex.
DR DIP; DIP-9265N; -.
DR IntAct; P69791; 12.
DR STRING; 511145.b1736; -.
DR TCDB; 4.A.3.2.1; the pts lactose-n,n'-diacetylchitobiose-Beta-glucoside (lac) family.
DR iPTMnet; P69791; -.
DR PaxDb; P69791; -.
DR PRIDE; P69791; -.
DR EnsemblBacteria; AAC74806; AAC74806; b1736.
DR EnsemblBacteria; BAA15517; BAA15517; BAA15517.
DR GeneID; 67415560; -.
DR GeneID; 946244; -.
DR KEGG; ecj:JW1725; -.
DR KEGG; eco:b1736; -.
DR PATRIC; fig|1411691.4.peg.520; -.
DR EchoBASE; EB0140; -.
DR eggNOG; COG1447; Bacteria.
DR HOGENOM; CLU_152490_3_0_6; -.
DR InParanoid; P69791; -.
DR OMA; MEQSRMA; -.
DR PhylomeDB; P69791; -.
DR BioCyc; EcoCyc:CELC-MON; -.
DR BioCyc; MetaCyc:CELC-MON; -.
DR EvolutionaryTrace; P69791; -.
DR PRO; PR:P69791; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
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 CDD; cd00215; PTS_IIA_lac; 1.
DR InterPro; IPR003188; PTS_IIA_lac/cel.
DR InterPro; IPR036542; PTS_IIA_lac/cel_sf.
DR PANTHER; PTHR34382; PTHR34382; 1.
DR Pfam; PF02255; PTS_IIA; 1.
DR PIRSF; PIRSF000699; PTS_IILac_III; 1.
DR SUPFAM; SSF46973; SSF46973; 1.
DR TIGRFAMs; TIGR00823; EIIA-LAC; 1.
DR PROSITE; PS51095; PTS_EIIA_TYPE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..116
FT /note="PTS system N,N'-diacetylchitobiose-specific EIIA
FT component"
FT /id="PRO_0000186494"
FT DOMAIN 15..113
FT /note="PTS EIIA type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
FT ACT_SITE 89
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000305|PubMed:15654077,
FT ECO:0000305|PubMed:19959833, ECO:0000305|PubMed:2092358,
FT ECO:0000305|PubMed:22593574"
FT MOD_RES 89
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00418,
FT ECO:0000305|PubMed:10913118, ECO:0000305|PubMed:15654077,
FT ECO:0000305|PubMed:22593574"
FT VARIANT 14
FT /note="A -> V (in strain: ECOR 1)"
FT VARIANT 52
FT /note="A -> T (in strain: ECOR 61)"
FT VARIANT 59
FT /note="M -> I (in strain: ECOR 50)"
FT MUTAGEN 92
FT /note="D->L: Eliminates the need for a metal cation at the
FT homotrimer interface by substituting hydrophobic methyl-
FT methyl interactions in place of the metal cation."
FT /evidence="ECO:0000269|PubMed:15654077"
FT CONFLICT 43..44
FT /note="KQ -> NR (in Ref. 1; CAA37071)"
FT /evidence="ECO:0000305"
FT HELIX 15..43
FT /evidence="ECO:0007829|PDB:1WCR"
FT HELIX 47..74
FT /evidence="ECO:0007829|PDB:1WCR"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1WCR"
FT HELIX 85..114
FT /evidence="ECO:0007829|PDB:1WCR"
SQ SEQUENCE 116 AA; 12748 MW; F2951DC6700FA8A9 CRC64;
MMDLDNIPDT QTEAEELEEV VMGLIINSGQ ARSLAYAALK QAKQGDFAAA KAMMDQSRMA
LNEAHLVQTK LIEGDAGEGK MKVSLVLVHA QDHLMTSMLA RELITELIEL HEKLKA
