PTQC_ECOLI
ID PTQC_ECOLI Reviewed; 452 AA.
AC P17334; P76212; P76907; P77332;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=PTS system N,N'-diacetylchitobiose-specific EIIC component {ECO:0000303|PubMed:2092358};
DE AltName: Full=EIIC-Chb {ECO:0000303|PubMed:2092358};
DE AltName: Full=IIcel {ECO:0000303|PubMed:2179047};
DE AltName: Full=N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIC component {ECO:0000303|PubMed:2092358};
GN Name=chbC {ECO:0000303|PubMed:9405618};
GN Synonyms=celB {ECO:0000303|PubMed:2179047};
GN OrderedLocusNames=b1737, JW1726;
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, INDUCTION, AND SUBSTRATE SPECIFICITY.
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.
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 TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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 {ECO:0000269|PubMed:10913117, ECO:0000305|PubMed:2092358}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00428}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00428}.
CC -!- INDUCTION: By GlcNAc2, GlcNAc3 and beta-N,N'-diacetylchitobiose (Me-
CC TCB). {ECO:0000269|PubMed:10913117}.
CC -!- DOMAIN: The EIIC type-3 domain forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00428}.
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; CAA37070.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74807.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15518.1; -; Genomic_DNA.
DR PIR; A64933; A64933.
DR PIR; S10871; S10871.
DR RefSeq; NP_416251.1; NC_000913.3.
DR RefSeq; WP_000073041.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P17334; -.
DR SMR; P17334; -.
DR BioGRID; 4260315; 20.
DR ComplexPortal; CPX-4683; N,N'-diacetylchitobiose-specific enzyme II complex.
DR DIP; DIP-9264N; -.
DR IntAct; P17334; 1.
DR STRING; 511145.b1737; -.
DR TCDB; 4.A.3.2.1; the pts lactose-n,n'-diacetylchitobiose-Beta-glucoside (lac) family.
DR PaxDb; P17334; -.
DR PRIDE; P17334; -.
DR EnsemblBacteria; AAC74807; AAC74807; b1737.
DR EnsemblBacteria; BAA15518; BAA15518; BAA15518.
DR GeneID; 66674368; -.
DR GeneID; 945982; -.
DR KEGG; ecj:JW1726; -.
DR KEGG; eco:b1737; -.
DR PATRIC; fig|1411691.4.peg.519; -.
DR EchoBASE; EB0139; -.
DR eggNOG; COG1455; Bacteria.
DR InParanoid; P17334; -.
DR OMA; EMFTFVV; -.
DR PhylomeDB; P17334; -.
DR BioCyc; EcoCyc:CELB-MON; -.
DR BioCyc; MetaCyc:CELB-MON; -.
DR PRO; PR:P17334; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:1901264; P:carbohydrate derivative transport; IBA:GO_Central.
DR GO; GO:1902815; P:N,N'-diacetylchitobiose import; IDA:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IC:ComplexPortal.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR004501; PTS_EIIC_3.
DR InterPro; IPR004796; PTS_IIC_cello.
DR Pfam; PF02378; PTS_EIIC; 1.
DR PIRSF; PIRSF006351; PTS_EIIC-Cellobiose; 1.
DR TIGRFAMs; TIGR00359; cello_pts_IIC; 1.
DR TIGRFAMs; TIGR00410; lacE; 1.
DR PROSITE; PS51105; PTS_EIIC_TYPE_3; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..452
FT /note="PTS system N,N'-diacetylchitobiose-specific EIIC
FT component"
FT /id="PRO_0000186485"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TOPO_DOM 56..85
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TOPO_DOM 107..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TOPO_DOM 135..146
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TOPO_DOM 168..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TOPO_DOM 208..228
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TOPO_DOM 250..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TOPO_DOM 321..343
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TOPO_DOM 365..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TOPO_DOM 388..408
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TOPO_DOM 430..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 8..426
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT CONFLICT 190..205
FT /note="LIPGFIILSVMGIIAW -> FNSRLYYSFRDGDYCL (in Ref. 1;
FT CAA37070)"
FT /evidence="ECO:0000305"
FT CONFLICT 233..235
FT /note="VGW -> WL (in Ref. 1; CAA37070)"
FT /evidence="ECO:0000305"
FT CONFLICT 240..265
FT /note="FVPLLWFFGIHGALALTALDNGIMTP -> LSTALVLRIHAACADRTGQRHY
FT DA (in Ref. 1; CAA37070)"
FT /evidence="ECO:0000305"
FT CONFLICT 361..366
FT /note="FVLVQP -> LYWYNR (in Ref. 1; CAA37070)"
FT /evidence="ECO:0000305"
FT CONFLICT 405..452
FT /note="SVAALLVALFNLGIATLIYLPFVVVANKAQNAIDKEESEEDIANALKF ->
FT TSPHCWSHSSTLASQR (in Ref. 1; CAA37070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 48332 MW; EC3CBFEED6231068 CRC64;
MSNVIASLEK VLLPFAVKIG KQPHVNAIKN GFIRLMPLTL AGAMFVLINN VFLSFGEGSF
FYSLGIRLDA STIETLNGLK GIGGNVYNGT LGIMSLMAPF FIGMALAEER KVDALAAGLL
SVAAFMTVTP YSVGEAYAVG ANWLGGANII SGIIIGLVVA EMFTFIVRRN WVIKLPDSVP
ASVSRSFSAL IPGFIILSVM GIIAWALNTW GTNFHQIIMD TISTPLASLG SVVGWAYVIF
VPLLWFFGIH GALALTALDN GIMTPWALEN IATYQQYGSV EAALAAGKTF HIWAKPMLDS
FIFLGGSGAT LGLILAIFIA SRRADYRQVA KLALPSGIFQ INEPILFGLP IIMNPVMFIP
FVLVQPILAA ITLAAYYMGI IPPVTNIAPW TMPTGLGAFF NTNGSVAALL VALFNLGIAT
LIYLPFVVVA NKAQNAIDKE ESEEDIANAL KF
