PTQB_ECO57
ID PTQB_ECO57 Reviewed; 106 AA.
AC P69830; P17409;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=PTS system N,N'-diacetylchitobiose-specific EIIB component {ECO:0000250|UniProtKB:P69795};
DE AltName: Full=EIIB-Chb {ECO:0000250|UniProtKB:P69795};
DE AltName: Full=IVcel {ECO:0000250|UniProtKB:P69795};
DE AltName: Full=N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P69795};
DE EC=2.7.1.196 {ECO:0000250|UniProtKB:P69795};
GN Name=chbB; Synonyms=celA; OrderedLocusNames=Z2768, ECs2444;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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).
CC {ECO:0000250|UniProtKB:P69795}.
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:0000250|UniProtKB:P69795};
CC -!- SUBUNIT: Forms a complex with ChbA (EIIA). ChbB is a monomer in both
CC its unphosphorylated and phosphorylated forms.
CC {ECO:0000250|UniProtKB:P69795}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By GlcNAc2, GlcNAc3 and beta-N,N'-diacetylchitobiose (Me-
CC TCB). {ECO:0000250|UniProtKB:P69795}.
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}.
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DR EMBL; AE005174; AAG56724.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35867.1; -; Genomic_DNA.
DR PIR; D90934; D90934.
DR PIR; H85782; H85782.
DR RefSeq; NP_310471.1; NC_002695.1.
DR RefSeq; WP_000412169.1; NZ_SWKA01000004.1.
DR AlphaFoldDB; P69830; -.
DR BMRB; P69830; -.
DR SMR; P69830; -.
DR STRING; 155864.EDL933_2697; -.
DR EnsemblBacteria; AAG56724; AAG56724; Z2768.
DR EnsemblBacteria; BAB35867; BAB35867; ECs_2444.
DR GeneID; 67415558; -.
DR GeneID; 912602; -.
DR KEGG; ece:Z2768; -.
DR KEGG; ecs:ECs_2444; -.
DR PATRIC; fig|386585.9.peg.2558; -.
DR eggNOG; COG1440; Bacteria.
DR HOGENOM; CLU_147323_2_0_6; -.
DR OMA; DAEIFAC; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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 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 3: Inferred from homology;
KW 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_0000186491"
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:0000250|UniProtKB:P69795"
FT MOD_RES 10
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
SQ SEQUENCE 106 AA; 11427 MW; DE4AADE300D18F53 CRC64;
MEKKHIYLFC SAGMSTSLLV SKMRAQAEKY EVPVIIEAFP ETLAGEKGQN ADVVLLGPQI
AYMLPEIQRL LPNKPVEVID SLLYGKVDGL GVLKAAVAAI KKAAAN
